1ttg: Difference between revisions
New page: left|200px<br /> <applet load="1ttg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ttg" /> '''THE THREE-DIMENSIONAL STRUCTURE OF THE TENT... |
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[[Image:1ttg.gif|left|200px]]<br /> | [[Image:1ttg.gif|left|200px]]<br /><applet load="1ttg" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''THE THREE-DIMENSIONAL STRUCTURE OF THE TENTH TYPE III MODULE OF FIBRONECTIN: AN INSIGHT INTO RGD-MEDIATED INTERACTIONS'''<br /> | '''THE THREE-DIMENSIONAL STRUCTURE OF THE TENTH TYPE III MODULE OF FIBRONECTIN: AN INSIGHT INTO RGD-MEDIATED INTERACTIONS'''<br /> | ||
==Overview== | ==Overview== | ||
The solution structure of the tenth type III module of fibronectin has | 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. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1TTG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1TTG is a [http://en.wikipedia.org/wiki/Single_protein 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=1TTG OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Baron, M.]] | [[Category: Baron, M.]] | ||
[[Category: Campbell, I | [[Category: Campbell, I D.]] | ||
[[Category: Harvey, T | [[Category: Harvey, T S.]] | ||
[[Category: Main, A | [[Category: Main, A L.]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:08 2008'' | ||
Revision as of 13:17, 21 February 2008
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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.
Disease
Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[135600]
About this Structure
1TTG 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
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