1fuv
From Proteopedia
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| - | [[Image:1fuv.jpg|left|200px]] | + | [[Image:1fuv.jpg|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF AN RGD PEPTIDE ISOMER-A''' | + | {{Structure |
| + | |PDB= 1fuv |SIZE=350|CAPTION= <scene name='initialview01'>1fuv</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF AN RGD PEPTIDE ISOMER-A''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FUV is a [ | + | 1FUV is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUV OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structures and integrin binding activities of an RGD peptide with two isomers., Assa-Munt N, Jia X, Laakkonen P, Ruoslahti E, Biochemistry. 2001 Feb 27;40(8):2373-8. PMID:[http:// | + | Solution structures and integrin binding activities of an RGD peptide with two isomers., Assa-Munt N, Jia X, Laakkonen P, Ruoslahti E, Biochemistry. 2001 Feb 27;40(8):2373-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11327857 11327857] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Assa-Munt, N.]] | [[Category: Assa-Munt, N.]] | ||
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[[Category: Laakkonen, P.]] | [[Category: Laakkonen, P.]] | ||
[[Category: Ruoslahti, E.]] | [[Category: Ruoslahti, E.]] | ||
| - | [[Category: double s-s | + | [[Category: double s-s bond]] |
[[Category: type i beta-turn]] | [[Category: type i beta-turn]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:14:18 2008'' |
Revision as of 09:14, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF AN RGD PEPTIDE ISOMER-A
Overview
The Arg-Gly-Asp (RGD) sequence serves as the primary integrin recognition site in extracellular matrix proteins, and peptides containing this sequence can mimic the activities of the matrix proteins. Depending on the context of the RGD sequence, an RGD-containing peptide may bind to all of the RGD-directed integrins, to a few, or to only a single one. We have previously isolated from a phage-displayed peptide library a cyclic peptide that binds avidly to the alpha(v)beta3 and alpha(v)beta5 integrins but does not bind to other closely related integrins. This peptide, ACDCRGDCFCG, exists in two natural configurations depending on internal disulfide bonding. The peptide with the 1-4; 2-3 disulfide bond arrangement accounts for most of the alpha(v) integrin binding activity, whereas the 1-3; 2-4 peptide is about 10-fold less potent. Solution structure analysis by nuclear magnetic resonance reveals an entirely different presentation of the RGD motif in the two isomers of RGD-4C. These results provide new insight into the ligand recognition specificity of integrins.
About this Structure
1FUV is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Solution structures and integrin binding activities of an RGD peptide with two isomers., Assa-Munt N, Jia X, Laakkonen P, Ruoslahti E, Biochemistry. 2001 Feb 27;40(8):2373-8. PMID:11327857
Page seeded by OCA on Thu Mar 20 11:14:18 2008
