1rmf
From Proteopedia
|
STRUCTURES OF A MONOCLONAL ANTI-ICAM-1 ANTIBODY R6.5 FRAGMENT AT 2.8 ANGSTROMS RESOLUTION
Overview
The specific binding of the monoclonal murine anti-intercellular adhesion, molecule-1 (anti-ICAM-1) antibody, R6.5, inhibits the attachment of, neutrophils to endothelium and prevents the attachment of major group, human rhinovirus (HRV) to ICAM-1. This binding interferes with the host, immune system and, as a result, the R6.5 antibody has been developed as a, therapeutic anti-inflammatory and perhaps anti-HRV agent. The, variable-region amino-acid sequence of R6.5 was determined from the, anti-ICAM-1 cDNA. The crystallization conditions of the Fab fragment of, R6.5 were established and the three-dimensional structure was determined, by X-ray crystallography. The crystal space group is orthorhombic, P2(1)2(1)2(1), a = 40.36, b = 137.76, c = 91.32 A, and the highest, resolution of recorded reflections is 2.7 A. The molecular-replacement, method using known Fab structures was employed to solve the R6.5 Fab, structure. The final R-factor is 18.8% for a total of 3320 non-H protein, atoms, 39 water molecules and 10 606 unique reflections. The protein, exhibits the typical immunoglobulin fold. The surface contour of the, antigen-combining site of the R6.5 antibody has a wide groove which, resembles more the structure of an anti-polypeptide antibody than the, structure of an anti-protein antibody.
About this Structure
1RMF is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structure of a monoclonal anti-ICAM-1 antibody R6.5 Fab fragment at 2.8 A resolution., Jedrzejas MJ, Miglietta J, Griffin JA, Luo M, Acta Crystallogr D Biol Crystallogr. 1995 May 1;51(Pt 3):380-5. PMID:15299305
Page seeded by OCA on Sun Nov 18 09:41:32 2007
