1FUV: SOLUTION STRUCTURE OF AN RGD PEPTIDE ISOMER-A

Citation:
Abstract
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.
PDB ID: 1FUVDownload
MMDB ID: 72090
PDB Deposition Date: 2000/9/15
Updated in MMDB: 2009/07
Experimental Method:
solution nmr
Similar Structures:
Molecular Components in 1FUV
Label Count Molecule
Protein (1 molecule)
1
RGD Peptide Isomer-a
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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