1VSC

VCAM-1

Summary for 1VSC

• Entry DOI: 10.2210/pdb1vsc/pdb
• Descriptor: VASCULAR CELL ADHESION MOLECULE-1 (2 entities in total)
• Functional Keywords: cell adhesion protein, immunoglobulin fold, glycoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P19320
• Total number of polymer chains: 2
• Total formula weight: 43691.50

Authors

Wang, J.,Stehle, T.,Osborn, L. (deposition date: 1995-04-27, release date: 1996-06-20, Last modification date: 2024-10-23)

Primary citation

Wang, J.H.,Pepinsky, R.B.,Stehle, T.,Liu, J.H.,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.USA, 92:5714-5718, 1995

PubMed Abstract: 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.

PubMed: 7539925
DOI: 10.1073/pnas.92.12.5714

Experimental method

X-RAY DIFFRACTION (1.9 Å)