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1vsc

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1vsc, resolution 1.90Å ()
Gene: VCAM-D1D2-IG (Homo sapiens)
Domains: C2-set, IGcam
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



VCAM-1

Publication Abstract from PubMed

Vascular cell adhesion molecule 1 (VCAM-1) represents a structurally and functionally distinct class of immunoglobulin superfamily molecules that bind leukocyte integrins and are involved in inflammatory and immune functions. X-ray crystallography defines the three-dimensional structure of the N-terminal two-domain fragment that participates in ligand binding. Residues in domain 1 important for ligand binding reside in the C-D loop, which projects markedly from one face of the molecule near the contact between domains 1 and 2. A cyclic peptide that mimics this loop inhibits binding of alpha 4 beta 1 integrin-bearing cells to VCAM-1. These data demonstrate how crystallographic structural information can be used to design a small molecule inhibitor of biological function.

The crystal structure of an N-terminal two-domain fragment of vascular cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1-alpha 4 integrin interaction., Wang JH, Pepinsky RB, Stehle T, Liu JH, Karpusas M, Browning B, Osborn L, Proc Natl Acad Sci U S A. 1995 Jun 6;92(12):5714-8. PMID:7539925

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1VSC is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Wang JH, Pepinsky RB, Stehle T, Liu JH, Karpusas M, Browning B, Osborn L. The crystal structure of an N-terminal two-domain fragment of vascular cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1-alpha 4 integrin interaction. Proc Natl Acad Sci U S A. 1995 Jun 6;92(12):5714-8. PMID:7539925

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