1fna
From Proteopedia
(New page: 200px<br /> <applet load="1fna" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fna, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF...) |
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caption="1fna, resolution 1.8Å" /> | caption="1fna, resolution 1.8Å" /> | ||
'''CRYSTAL STRUCTURE OF THE TENTH TYPE III CELL ADHESION MODULE OF HUMAN FIBRONECTIN'''<br /> | '''CRYSTAL STRUCTURE OF THE TENTH TYPE III CELL ADHESION MODULE OF HUMAN FIBRONECTIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the cell adhesion module of fibronectin (FNIII10) | + | The crystal structure of the cell adhesion module of fibronectin (FNIII10) has been determined at 1.8 A resolution. A recombinant fragment corresponding to the tenth type III module of human fibronectin was crystallized in space group P2(1) with a = 30.7, b = 35.1 and c = 37.7 A and beta = 107 degrees. The structure was determined by molecular replacement and refined by least squares methods. The crystallographic R-factor for the final model of the 91 amino acid module plus 56 solvent atoms is 0.18 for 10 to 1.8 A data. The module consists of two layers of beta-sheet, one with three antiparallel strands and the other with four antiparallel strands. The beta-sheets enclose a hydrophobic core of 24 amino acid side-chains. The module contains the RGD cell recognition sequence in a flexible loop connecting two beta-strands. The tertiary structure of the FNIII10 module has been used to develop a structure-based sequence alignment of 17 type III modules in fibronectin based on the striking conservation of homologous hydrophobic residues. A similar pattern of homologous alternating hydrophobic residues is also evident in a comparison of type III modules in proteins unrelated to fibronectin such as cytokine receptors and muscle proteins. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FNA 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:// | + | 1FNA 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=1FNA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dickinson, C | + | [[Category: Dickinson, C D.]] |
| - | [[Category: Ely, K | + | [[Category: Ely, K R.]] |
[[Category: Veerapandian, B.]] | [[Category: Veerapandian, B.]] | ||
[[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 12:40:30 2008'' |
Revision as of 10:40, 21 February 2008
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CRYSTAL STRUCTURE OF THE TENTH TYPE III CELL ADHESION MODULE OF HUMAN FIBRONECTIN
Contents |
Overview
The crystal structure of the cell adhesion module of fibronectin (FNIII10) has been determined at 1.8 A resolution. A recombinant fragment corresponding to the tenth type III module of human fibronectin was crystallized in space group P2(1) with a = 30.7, b = 35.1 and c = 37.7 A and beta = 107 degrees. The structure was determined by molecular replacement and refined by least squares methods. The crystallographic R-factor for the final model of the 91 amino acid module plus 56 solvent atoms is 0.18 for 10 to 1.8 A data. The module consists of two layers of beta-sheet, one with three antiparallel strands and the other with four antiparallel strands. The beta-sheets enclose a hydrophobic core of 24 amino acid side-chains. The module contains the RGD cell recognition sequence in a flexible loop connecting two beta-strands. The tertiary structure of the FNIII10 module has been used to develop a structure-based sequence alignment of 17 type III modules in fibronectin based on the striking conservation of homologous hydrophobic residues. A similar pattern of homologous alternating hydrophobic residues is also evident in a comparison of type III modules in proteins unrelated to fibronectin such as cytokine receptors and muscle proteins.
Disease
Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[135600]
About this Structure
1FNA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the tenth type III cell adhesion module of human fibronectin., Dickinson CD, Veerapandian B, Dai XP, Hamlin RC, Xuong NH, Ruoslahti E, Ely KR, J Mol Biol. 1994 Mar 4;236(4):1079-92. PMID:8120888
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