1koe
From Proteopedia
(Difference between revisions)
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<StructureSection load='1koe' size='340' side='right'caption='[[1koe]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1koe' size='340' side='right'caption='[[1koe]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1koe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1koe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KOE FirstGlance]. <br> |
- | </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=1koe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koe OCA], [https://pdbe.org/1koe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1koe RCSB], [https://www.ebi.ac.uk/pdbsum/1koe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1koe ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</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=1koe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koe OCA], [https://pdbe.org/1koe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1koe RCSB], [https://www.ebi.ac.uk/pdbsum/1koe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1koe ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/COIA1_MOUSE COIA1_MOUSE] Endostatin potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1koe ConSurf]. | </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=1koe ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | A number of extracellular proteins contain cryptic inhibitors of angiogenesis. Endostatin is a 20 kDa C-terminal proteolytic fragment of collagen XVIII that potently inhibits endothelial cell proliferation and angiogenesis. Therapy of experimental cancer with endostatin leads to tumour dormancy and does not induce resistance. We have expressed recombinant mouse endostatin and determined its crystal structure at 1.5 A resolution. The structure reveals a compact fold distantly related to the C-type lectin carbohydrate recognition domain and the hyaluronan-binding Link module. The high affinity of endostatin for heparin is explained by the presence of an extensive basic patch formed by 11 arginine residues. Endostatin may inhibit angiogenesis by binding to the heparan sulphate proteoglycans involved in growth factor signalling. | ||
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- | Crystal structure of the angiogenesis inhibitor endostatin at 1.5 A resolution.,Hohenester E, Sasaki T, Olsen BR, Timpl R EMBO J. 1998 Mar 16;17(6):1656-64. PMID:9501087<ref>PMID:9501087</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1koe" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Mus musculus]] |
- | [[Category: Hohenester | + | [[Category: Hohenester E]] |
- | [[Category: Olsen | + | [[Category: Olsen BR]] |
- | [[Category: Sasaki | + | [[Category: Sasaki T]] |
- | [[Category: Timpl | + | [[Category: Timpl R]] |
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Revision as of 08:02, 3 April 2024
ENDOSTATIN
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