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1ttg

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(New page: 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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'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TTG OCA].
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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.]]
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[[Category: Campbell, I.D.]]
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[[Category: Campbell, I D.]]
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[[Category: Harvey, T.S.]]
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[[Category: Harvey, T S.]]
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[[Category: Main, A.L.]]
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[[Category: Main, A L.]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]
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''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

Image:1ttg.gif

1ttg

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THE THREE-DIMENSIONAL STRUCTURE OF THE TENTH TYPE III MODULE OF FIBRONECTIN: AN INSIGHT INTO RGD-MEDIATED INTERACTIONS

Contents

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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