Low Resolution Solution Structure of HAMLET and the Importance of Its Alpha-Domains in Tumoricidal Activity
Publication Date
December 27, 2012
Journal
PLOS ONE
Authors
James Ho Cs, Anna Rydstrom, Malathy Sony Subramanian Manimekalai, Catharina Svanborg, et al
Volume
7
Issue
12
Pages
e53051
DOI
https://dx.plos.org/10.1371/journal.pone.0053051
Publisher URL
http://journals.plos.org/plosone/article?id=10.1371%2Fjournal.pone.0053051
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/23300861
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3531425
Europe PMC
http://europepmc.org/abstract/MED/23300861
Web of Science
000312829100114
Scopus
84871647785
Mendeley
http://www.mendeley.com/research/low-resolution-solution-structure-hamlet-importance-alphadomains-tumoricidal-activity
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Mendeley | Further Information

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Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/282547", "https://ndownloader.figshare.com/files/282585", "https://ndownloader.figshare.com/files/282624", "https://ndownloader.figshare.com/files/282706", "https://ndownloader.figshare.com/files/282737", "https://ndownloader.figshare.com/files/282784", "https://ndownloader.figshare.com/files/282820"], "description"=>"<div><p>HAMLET (<u>H</u>uman <u>A</u>lpha-lactalbumin <u>M</u>ade <u>LE</u>thal to <u>T</u>umor cells) is the first member in a new family of protein-lipid complexes with broad tumoricidal activity. Elucidating the molecular structure and the domains crucial for HAMLET formation is fundamental for understanding its tumoricidal function. Here we present the low-resolution solution structure of the complex of oleic acid bound HAMLET, derived from small angle X-ray scattering data. HAMLET shows a two-domain conformation with a large globular domain and an extended part of about 2.22 nm in length and 1.29 nm width. The structure has been superimposed into the related crystallographic structure of human α-lactalbumin, revealing that the major part of α-lactalbumin accommodates well in the shape of HAMLET. However, the C-terminal residues from L105 to L123 of the crystal structure of the human α-lactalbumin do not fit well into the HAMLET structure, resulting in an extended conformation in HAMLET, proposed to be required to form the tumoricidal active HAMLET complex with oleic acid. Consistent with this low resolution structure, we identified biologically active peptide epitopes in the globular as well as the extended domains of HAMLET. Peptides covering the alpha1 and alpha2 domains of the protein triggered rapid ion fluxes in the presence of sodium oleate and were internalized by tumor cells, causing rapid and sustained changes in cell morphology. The alpha peptide-oleate bound forms also triggered tumor cell death with comparable efficiency as HAMLET. In addition, shorter peptides corresponding to those domains are biologically active. These findings provide novel insights into the structural prerequisites for the dramatic effects of HAMLET on tumor cells.</p> </div>", "links"=>[], "tags"=>["hamlet", "alpha-domains", "tumoricidal", "activity"], "article_id"=>115712, "categories"=>["Biochemistry", "Biological Sciences", "Cancer", "Cell Biology", "Biophysics"], "users"=>["James Ho CS", "Anna Rydstrom", "Malathy Sony Subramanian Manimekalai", "Catharina Svanborg", "Gerhard Grüber"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0053051.s001", "https://dx.doi.org/10.1371/journal.pone.0053051.s002", "https://dx.doi.org/10.1371/journal.pone.0053051.s003", "https://dx.doi.org/10.1371/journal.pone.0053051.s004", "https://dx.doi.org/10.1371/journal.pone.0053051.s005", "https://dx.doi.org/10.1371/journal.pone.0053051.s006", "https://dx.doi.org/10.1371/journal.pone.0053051.s007"], "stats"=>{"downloads"=>0, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Low_Resolution_Solution_Structure_of_HAMLET_and_the_Importance_of_Its_Alpha_Domains_in_Tumoricidal_Activity__/115712", "title"=>"Low Resolution Solution Structure of HAMLET and the Importance of Its Alpha-Domains in Tumoricidal Activity", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-12-27 01:35:12"}
  • {"files"=>["https://ndownloader.figshare.com/files/518284"], "description"=>"<p>Data-collection and scattering-derived parameters.</p>", "links"=>[], "tags"=>["scattering-derived"], "article_id"=>188778, "categories"=>["Biochemistry", "Biological Sciences", "Cancer", "Cell Biology", "Biophysics"], "users"=>["James Ho CS", "Anna Rydstrom", "Malathy Sony Subramanian Manimekalai", "Catharina Svanborg", "Gerhard Grüber"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0053051.t001", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Data_collection_and_scattering_derived_parameters_/188778", "title"=>"Data-collection and scattering-derived parameters.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2012-12-27 02:26:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/517761"], "description"=>"<p>(A) Amino acid sequence and secondary structure of human α-lactalbumin as well as the peptide domains alpha1, alpha2 and beta. (B) The three peptide domains in the crystallographic structure of human α-lactalbumin (PDB id: 1B9O <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0053051#pone.0053051-Svergun1\" target=\"_blank\">[21]</a>) (C), which is superimposed into the solution shape of HAMLET (C). (D) Surface representation showing the low resolution structure of the human α-lactalbumin with the three domains; alpha 1 in red, alpha 2 in blue and beta in gray color. The tail region of the SAXS shape, which is modeled on to the alpha2 domain low resolution structure, is also shown in blue.</p>", "links"=>[], "tags"=>["Computational biology", "cell biology", "oncology", "biophysics", "Biochemistry"], "article_id"=>188253, "categories"=>["Biochemistry", "Biological Sciences", "Cancer", "Cell Biology", "Biophysics"], "users"=>["James Ho CS", "Anna Rydstrom", "Malathy Sony Subramanian Manimekalai", "Catharina Svanborg", "Gerhard Grüber"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0053051.g003", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Peptide_sequences_/188253", "title"=>"Peptide sequences.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:17:33"}
  • {"files"=>["https://ndownloader.figshare.com/files/517653"], "description"=>"<p>(<i>A</i>) Low resolution structures of HAMLET in brown spheres and (<i>B</i>) its 180° view. (<i>C–D</i>) Superposition of HAMLET with human α-lactalbumin (PDB id: 1B9O <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0053051#pone.0053051-Svergun1\" target=\"_blank\">[21]</a>). The C-terminal residues from L105 to L123 of the crystal structure of the human α-lactalbumin, which form a flexible loop in the crystal structure of human α-lactalbumin, are colored red. We suggest that this region L105 to L123 takes up an extended conformation in HAMLET by forming a tail.</p>", "links"=>[], "tags"=>["hamlet"], "article_id"=>188149, "categories"=>["Biochemistry", "Biological Sciences", "Cancer", "Cell Biology", "Biophysics"], "users"=>["James Ho CS", "Anna Rydstrom", "Malathy Sony Subramanian Manimekalai", "Catharina Svanborg", "Gerhard Grüber"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0053051.g002", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SAXS_structure_of_HAMLET_and_native_human_945_lactalbumin_crystal_structure_/188149", "title"=>"SAXS structure of HAMLET and native human α-lactalbumin crystal structure.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:15:49"}
  • {"files"=>["https://ndownloader.figshare.com/files/517541"], "description"=>"<p>(A) Experimental scattering curves (o) with error bars in gray color and (<i>insert</i>) the Guinier plot with the linear fit (red line) are shown. (B) The fitting curves (—; <i>green</i>: fit for the experimental data, <i>red</i>: fit for the calculated <i>ab initio</i> model) of HAMLET derived from SAXS data. (C) Distance distribution functions of HAMLET. (D) The Kratky plot indicates that the protein is globular and folded. The increase at higher angles might reflect that the protein is slightly flexible.</p>", "links"=>[], "tags"=>["Computational biology", "cell biology", "oncology", "biophysics", "Biochemistry"], "article_id"=>188029, "categories"=>["Biochemistry", "Biological Sciences", "Cancer", "Cell Biology", "Biophysics"], "users"=>["James Ho CS", "Anna Rydstrom", "Malathy Sony Subramanian Manimekalai", "Catharina Svanborg", "Gerhard Grüber"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0053051.g001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SAXS_structure_analysis_/188029", "title"=>"SAXS structure analysis.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:13:49"}
  • {"files"=>["https://ndownloader.figshare.com/files/518025"], "description"=>"<p>(A) Peptides trigger ion fluxes in tumor cells. The free intracellular concentration of Na<sup>+</sup>, K<sup>+</sup> and Ca<sup>2+</sup> were measured by fluorescence spectrometry using CoroNa Green, FluxOR and Fluo-4, respectively. HAMLET, alpha1 peptide+oleate and alpha2 peptide+oleate mixtures trigger rapid fluxes of all three ions. Intracellular potassium ion concentrations were reduced due to ion efflux, while those of sodium and calcium were increased. Mean of at least two experiments. P values are explained in the text. (B) Peptide-oleate mixtures kill tumor cells. A549 lung carcinoma cells and Jurkat leukemia cells were incubated with HAMLET, oleate or peptide-oleate mixtures for 3 hours. Cell death was quantified as ATP levels and PrestoBlue, in % of control.</p>", "links"=>[], "tags"=>["fluxes"], "article_id"=>188522, "categories"=>["Biochemistry", "Biological Sciences", "Cancer", "Cell Biology", "Biophysics"], "users"=>["James Ho CS", "Anna Rydstrom", "Malathy Sony Subramanian Manimekalai", "Catharina Svanborg", "Gerhard Grüber"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0053051.g005", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Ion_fluxes_and_tumor_cell_death_/188522", "title"=>"Ion fluxes and tumor cell death.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:22:02"}
  • {"files"=>["https://ndownloader.figshare.com/files/518169"], "description"=>"<p>(A) Internalization of biotinylated peptides (red) by A549 lung carcinoma cells counterstained with WGA (green) and Hoechst (blue) and examined by confocal microscopy. Peptides 1,10 and 11 were internalized in the absence of oleate and peptides 10 and 11 also in the presence of oleate. (B) K<sup>+</sup> and (C) Ca<sup>2+</sup>fluxes in tumor cells triggered by petides 1, 10 and 11 were measured by fluorescence spectrometry. Peptides 10 and 11 triggered Ca<sup>2+</sup> fluxes, in the presence and absence of oleate and peptide 6 a weaker Ca<sup>2+</sup> flux with oleate. (D) Insignificant Na<sup>+</sup> fluxes.</p>", "links"=>[], "tags"=>["peptides", "induction", "ion"], "article_id"=>188664, "categories"=>["Biochemistry", "Biological Sciences", "Cancer", "Cell Biology", "Biophysics"], "users"=>["James Ho CS", "Anna Rydstrom", "Malathy Sony Subramanian Manimekalai", "Catharina Svanborg", "Gerhard Grüber"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0053051.g006", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Internalization_of_small_peptides_and_induction_of_ion_fluxes_/188664", "title"=>"Internalization of small peptides and induction of ion fluxes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:24:24"}
  • {"files"=>["https://ndownloader.figshare.com/files/517893"], "description"=>"<p>(A) Internalization of peptides. A549 lung carcinoma cells cultured on glass slides, were incubated with peptide-oleate mixtures for 1 hour, fixed and stained with AlexaFluor568-streptavidin, counterstained with WGA and examined by confocal microscopy. Alpha1 and alpha2 peptides, mixed with oleate, were internalized as shown by the red fluorescence. The beta peptide was not internalized. Scale bar 20 µm. (B) Morphological changes in A549 lung carcinoma cells treated with HAMLET, alpha1 peptide+oleate, alpha2 peptide+oleate and beta peptide+oleate recorded by holography imaging. Cells treated with HAMLET started to round up after 30 minutes and after 60 minutes, many cells had detached. Alpha1 peptide+oleate mixture triggers similar morphological changes as that by HAMLET. Alpha2 peptide+oleate mixture triggers similar morphological changes. Beta peptide+oleate mixture did not change cell morphology.</p>", "links"=>[], "tags"=>["peptides", "cells", "changes"], "article_id"=>188385, "categories"=>["Biochemistry", "Biological Sciences", "Cancer", "Cell Biology", "Biophysics"], "users"=>["James Ho CS", "Anna Rydstrom", "Malathy Sony Subramanian Manimekalai", "Catharina Svanborg", "Gerhard Grüber"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0053051.g004", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Internalization_of_peptides_into_tumor_cells_and_changes_in_tumor_cell_morphology_/188385", "title"=>"Internalization of peptides into tumor cells and changes in tumor cell morphology.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-12-27 02:19:45"}

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Relative Metric

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