3sh5
From Proteopedia
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- | [[ | + | ==Calcium-bound Laminin G like domain 3 from human perlecan== |
+ | <StructureSection load='3sh5' size='340' side='right' caption='[[3sh5]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3sh5]] is a 1 chain structure with 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=3SH5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SH5 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sh4|3sh4]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sh5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sh5 RCSB], [http://www.ebi.ac.uk/pdbsum/3sh5 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Endorepellin, the C-terminal region of perlecan, inhibits angiogenesis by disrupting actin cytoskeleton and focal adhesions. The C-terminal laminin-like globular domain (LG3) of endorepellin directs most of this antiangiogenic activity. To investigate the angiostatic mechanism and to identify structural determinants, we have solved crystal structures of the LG3 domain in both apo- and calcium-bound forms at resolutions of 1.5 A and 2.8 A, respectively. The conserved core has the jellyroll fold characteristic of LG domains. The calcium-induced structural changes seem very restricted, and the calcium binding site appears to be preformed, suggesting that the bound calcium ion, rather than structural rearrangements, contributes to antiangiogenesis. We have identified H4268 on the EF loop as a key residue for the biochemical function of LG3, since its mutation abolishes antiangiogenic activity, and mutant LG3 can no longer form a direct interaction with integrin. Taken together, we propose that these two distinct structural elements contribute to the angiostatic effect of endorepellin. | ||
- | + | Crystal Structure of the LG3 Domain of Endorepellin, an Angiogenesis Inhibitor.,V Le B, Kim H, Choi J, Kim JH, Hahn MJ, Lee C, Kim KK, Hwang HY J Mol Biol. 2011 Nov 25;414(2):231-42. Epub 2011 Oct 4. PMID:21996443<ref>PMID:21996443</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Kim, K K.]] | [[Category: Kim, K K.]] |
Revision as of 05:20, 5 June 2014
Calcium-bound Laminin G like domain 3 from human perlecan
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