1ttf
From Proteopedia
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'''THE THREE-DIMENSIONAL STRUCTURE OF THE TENTH TYPE III MODULE OF FIBRONECTIN: AN INSIGHT INTO RGD-MEDIATED INTERACTIONS''' | '''THE THREE-DIMENSIONAL STRUCTURE OF THE TENTH TYPE III MODULE OF FIBRONECTIN: AN INSIGHT INTO RGD-MEDIATED INTERACTIONS''' | ||
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[[Category: Harvey, T S.]] | [[Category: Harvey, T S.]] | ||
[[Category: Main, A L.]] | [[Category: Main, A L.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:20:30 2008'' | |
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Revision as of 07:20, 3 May 2008
THE THREE-DIMENSIONAL STRUCTURE OF THE TENTH TYPE III MODULE OF FIBRONECTIN: AN INSIGHT INTO RGD-MEDIATED INTERACTIONS
Overview
The solution structure of the tenth type III module of fibronectin has been determined using nuclear magnetic resonance techniques. The molecule has a fold similar to that of immunoglobulin domains, with seven beta strands forming two antiparallel beta sheets, which pack against each other. Both beta sheets contribute conserved hydrophobic residues to a compact core. The topology is more similar to that of domain 2 of CD4, PapD, and the extracellular domain of the human growth hormone receptor than to that of immunoglobulin C domains. The module contains an Arg-Gly-Asp sequence known to be involved in cell adhesion. This tripeptide is solvent exposed and lies on a conformationally mobile loop between strands F and G, consistent with its cell adhesion function.
About this Structure
1TTF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions., Main AL, Harvey TS, Baron M, Boyd J, Campbell ID, Cell. 1992 Nov 13;71(4):671-8. PMID:1423622 Page seeded by OCA on Sat May 3 10:20:30 2008
