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[[Image:1yo8.gif|left|200px]]
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{{STRUCTURE_1yo8|  PDB=1yo8  |  SCENE=  }}
'''Strucuture of the C-terminal domain of human thrombospondin-2'''


==Structure of the C-terminal domain of human thrombospondin-2==
<StructureSection load='1yo8' size='340' side='right'caption='[[1yo8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yo8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YO8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yo8 OCA], [https://pdbe.org/1yo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yo8 RCSB], [https://www.ebi.ac.uk/pdbsum/1yo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yo8 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/TSP2_HUMAN TSP2_HUMAN] Genetic variations in THBS2 may be a cause of susceptibility to intervertebral disk disease (IDD) [MIM:[https://omim.org/entry/603932 603932]; also known as lumbar disk herniation (LDH). IDD is one of the most common musculo-skeletal disorders and the predominant cause of low-back pain and unilateral leg pain.<ref>PMID:18455130</ref>
== Function ==
[https://www.uniprot.org/uniprot/TSP2_HUMAN TSP2_HUMAN] Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Ligand for CD36 mediating antiangiogenic properties.<ref>PMID:20714802</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yo/1yo8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yo8 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thrombospondins (THBSs) are secreted glycoproteins that have key roles in interactions between cells and the extracellular matrix. Here, we describe the 2.6-A-resolution crystal structure of the glycosylated signature domain of human THBS2, which includes three epidermal growth factor-like modules, 13 aspartate-rich repeats and a lectin-like module. These elements interact extensively to form three structural regions termed the stalk, wire and globe. The THBS2 signature domain is stabilized by these interactions and by a network of 30 bound Ca(2+) ions and 18 disulfide bonds. The structure suggests how genetic alterations of THBSs result in disease.


==Overview==
Structure of the calcium-rich signature domain of human thrombospondin-2.,Carlson CB, Bernstein DA, Annis DS, Misenheimer TM, Hannah BL, Mosher DF, Keck JL Nat Struct Mol Biol. 2005 Oct;12(10):910-4. Epub 2005 Sep 25. PMID:16186819<ref>PMID:16186819</ref>
Thrombospondins (THBSs) are secreted glycoproteins that have key roles in interactions between cells and the extracellular matrix. Here, we describe the 2.6-A-resolution crystal structure of the glycosylated signature domain of human THBS2, which includes three epidermal growth factor-like modules, 13 aspartate-rich repeats and a lectin-like module. These elements interact extensively to form three structural regions termed the stalk, wire and globe. The THBS2 signature domain is stabilized by these interactions and by a network of 30 bound Ca(2+) ions and 18 disulfide bonds. The structure suggests how genetic alterations of THBSs result in disease.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1YO8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YO8 OCA].
</div>
<div class="pdbe-citations 1yo8" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of the calcium-rich signature domain of human thrombospondin-2., Carlson CB, Bernstein DA, Annis DS, Misenheimer TM, Hannah BL, Mosher DF, Keck JL, Nat Struct Mol Biol. 2005 Oct;12(10):910-4. Epub 2005 Sep 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16186819 16186819]
*[[Thrombospondin|Thrombospondin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Annis, D S.]]
[[Category: Annis DS]]
[[Category: Bernstein, D A.]]
[[Category: Bernstein DA]]
[[Category: Carlson, C B.]]
[[Category: Carlson CB]]
[[Category: Hannah, B A.]]
[[Category: Hannah BA]]
[[Category: Keck, J L.]]
[[Category: Keck JL]]
[[Category: Misenheimer, T M.]]
[[Category: Misenheimer TM]]
[[Category: Mosher, D F.]]
[[Category: Mosher DF]]
[[Category: Disulfide]]
[[Category: Egf]]
[[Category: Lectin domain]]
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