6jza
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Fstl1== | |
| + | <StructureSection load='6jza' size='340' side='right'caption='[[6jza]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6jza]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JZA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JZA FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6jza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jza OCA], [http://pdbe.org/6jza PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jza RCSB], [http://www.ebi.ac.uk/pdbsum/6jza PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jza ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FSTL1_MOUSE FSTL1_MOUSE]] May modulate the action of some growth factors on cell proliferation and differentiation. Binds heparin (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fstl1 is a TGF-beta superfamily binding protein which involved in many pathological processes. The function of Fstl1 has been widely elucidated, but its structural characterization has not been explored. Here we solved the high-resolution crystal structure of FK domain of murine Fstl1, analyzed its unique characteristics, and investigated its contribution to the function of full-length Fstl1. We found that Fstl1-FK forms a stable dimer in both solution and crystal, which suggest that this protein may function as a dimer during its interaction with TGF-beta, a molecule known to form dimer during activation process. We also found this FK domain is indispensable for the proper function of Fstl1 during the transduction of TGF-beta signaling. These observations provide important insights into the understanding of Fstl1 and may facilitate the exploration of this molecule in clinical study. | ||
| - | + | Structural and functional study of FK domain of Fstl1.,Li X, Li L, Chang Y, Ning W, Liu X Protein Sci. 2019 Jul 27. doi: 10.1002/pro.3696. PMID:31351024<ref>PMID:31351024</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6jza" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Liu, X]] | [[Category: Liu, X]] | ||
[[Category: Ning, W]] | [[Category: Ning, W]] | ||
| + | [[Category: Antitumor protein]] | ||
| + | [[Category: Development]] | ||
| + | [[Category: Dimer]] | ||
| + | [[Category: Signaling]] | ||
| + | [[Category: Tgf]] | ||
Current revision
Structure of Fstl1
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Categories: Large Structures | Liu, X | Ning, W | Antitumor protein | Development | Dimer | Signaling | Tgf
