1fbr
From Proteopedia
(New page: 200px<br /> <applet load="1fbr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fbr" /> '''FOURTH AND FIFTH FIBRONECTIN TYPE I MODULE ...) |
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'''FOURTH AND FIFTH FIBRONECTIN TYPE I MODULE PAIR'''<br /> | '''FOURTH AND FIFTH FIBRONECTIN TYPE I MODULE PAIR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The tertiary structure of the fourth and fifth type 1 module pair from the | + | The tertiary structure of the fourth and fifth type 1 module pair from the N terminus of human fibronectin, has been determined by two-dimensional homonuclear 1H nuclear magnetic resonance (NMR) spectroscopy. Comparison of each module fold with those of two other type 1 modules shows that the type 1 "consensus" structure is conserved in the pair. The modules connect end-to-end to form an elongated structure with a limited clockwise twist around the long axis, from N to C terminus. The short five residue linker sequence forms a tight loop and the relative orientation of the two modules is maintained by fixed and intimate hydrophobic contacts, dominated by a non-conserved tryptophan residue from the fourth type 1 module. The protein binds specifically to fibrin in an ELISA and surface accessible residues that may be involved in this and other protein interactions can be identified. The structure provides an insight into how chains of type 1 modules may link up in intact fibronectin. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FBR 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:// | + | 1FBR 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=1FBR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Campbell, I | + | [[Category: Campbell, I D.]] |
| - | [[Category: Phan, I | + | [[Category: Phan, I Q.H.]] |
| - | [[Category: Williams, M | + | [[Category: Williams, M J.]] |
[[Category: cell adhesion protein]] | [[Category: cell adhesion protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:01 2008'' |
Revision as of 10:37, 21 February 2008
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FOURTH AND FIFTH FIBRONECTIN TYPE I MODULE PAIR
Contents |
Overview
The tertiary structure of the fourth and fifth type 1 module pair from the N terminus of human fibronectin, has been determined by two-dimensional homonuclear 1H nuclear magnetic resonance (NMR) spectroscopy. Comparison of each module fold with those of two other type 1 modules shows that the type 1 "consensus" structure is conserved in the pair. The modules connect end-to-end to form an elongated structure with a limited clockwise twist around the long axis, from N to C terminus. The short five residue linker sequence forms a tight loop and the relative orientation of the two modules is maintained by fixed and intimate hydrophobic contacts, dominated by a non-conserved tryptophan residue from the fourth type 1 module. The protein binds specifically to fibrin in an ELISA and surface accessible residues that may be involved in this and other protein interactions can be identified. The structure provides an insight into how chains of type 1 modules may link up in intact fibronectin.
Disease
Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[135600]
About this Structure
1FBR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of a pair of fibronectin type 1 modules with fibrin binding activity., Williams MJ, Phan I, Harvey TS, Rostagno A, Gold LI, Campbell ID, J Mol Biol. 1994 Jan 28;235(4):1302-11. PMID:8308892
Page seeded by OCA on Thu Feb 21 12:37:01 2008
