2fn2
From Proteopedia
(New page: 200px<br /> <applet load="2fn2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fn2" /> '''SOLUTION NMR STRUCTURE OF THE GLYCOSYLATED ...) |
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'''SOLUTION NMR STRUCTURE OF THE GLYCOSYLATED SECOND TYPE TWO MODULE OF FIBRONECTIN, 20 STRUCTURES'''<br /> | '''SOLUTION NMR STRUCTURE OF THE GLYCOSYLATED SECOND TYPE TWO MODULE OF FIBRONECTIN, 20 STRUCTURES'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2FN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FN2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: type two module]] | [[Category: type two module]] | ||
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Revision as of 15:25, 15 February 2008
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SOLUTION NMR STRUCTURE OF THE GLYCOSYLATED SECOND TYPE TWO MODULE OF FIBRONECTIN, 20 STRUCTURES
Contents |
Overview
Fibronectin is an extracellular matrix glycoprotein that plays a role in a, number of physiological processes involving cell adhesion and migration., The modules of the fibronectin monomer are organized into proteolytically, resistant domains that in isolation retain their affinity for various, ligands. The tertiary structure of the glycosylated second type 2 module, (2F2) from the gelatin-binding domain of fibronectin was determined by, two-dimensional nuclear magnetic resonance spectroscopy and simulated, annealing. The structure is well defined with an overall fold typical of, F2 modules, showing two double-stranded antiparallel beta-sheets and a, partially solvent-exposed hydrophobic cluster. An N-terminal beta-sheet, that was not present in previously determined F2 module structures, may be, important for defining the relative orientation of adjacent F2 modules in, fibronectin. This is the first three-dimensional structure of a, glycosylated module of fibronectin, and provides insight into the possible, role of the glycosylation in protein stability, protease resistance and, modulation of collagen binding. Based on the structures of the isolated, modules, models for the 1F22F2 pair were generated by randomly changing, the orientation of the linker peptide between the modules. The models, suggest that the two putative collagen binding sites in the pair form, discrete binding sites, rather than combining to form a single binding, site.
Disease
Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[135600]
About this Structure
2FN2 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of the glycosylated second type 2 module of fibronectin., Sticht H, Pickford AR, Potts JR, Campbell ID, J Mol Biol. 1998 Feb 13;276(1):177-87. PMID:9514732
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