1RMF

STRUCTURES OF A MONOCLONAL ANTI-ICAM-1 ANTIBODY R6.5 FRAGMENT AT 2.8 ANGSTROMS RESOLUTION

Summary for 1RMF

• Entry DOI: 10.2210/pdb1rmf/pdb
• Descriptor: IGG2A-KAPPA R6.5 FAB (LIGHT CHAIN), IGG2A-KAPPA R6.5 FAB (HEAVY CHAIN) (3 entities in total)
• Functional Keywords: immunoglobulin
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 47183.62

Authors

Jedrzejas, M.J.,Luo, M. (deposition date: 1994-12-16, release date: 1995-02-27, Last modification date: 2024-11-20)

Primary citation

Jedrzejas, M.J.,Miglietta, J.,Griffin, J.A.,Luo, M.
Structure of a monoclonal anti-ICAM-1 antibody R6.5 Fab fragment at 2.8 A resolution.
Acta Crystallogr.,Sect.D, 51:380-385, 1995

PubMed Abstract: 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.

PubMed: 15299305
DOI: 10.1107/S0907444994011054

Experimental method

X-RAY DIFFRACTION (2.8 Å)