PDBsum entry 1rmf

Immunoglobulin

PDB id: 1rmf

Contents

Protein chains

219 a.a. *

216 a.a. *

Waters ×117

* Residue conservation analysis

PDB id:

1rmf

Name:

Immunoglobulin

Title:

Structures of a monoclonal anti-icam-1 antibody r6.5 fragment at 2.8 angstroms resolution

Structure:

Igg2a-kappa r6.5 fab (light chain). Chain: l. Engineered: yes. Igg2a-kappa r6.5 fab (heavy chain). Chain: h. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Organism_taxid: 10090

Biol. unit:

Dimer (from PQS)

Resolution:

2.80Å R-factor: 0.188

Authors:

M.J.Jedrzejas,M.Luo

Key ref:

M.J.Jedrzejas et al. (1995). Structure of a monoclonal anti-ICAM-1 antibody R6.5 Fab fragment at 2.8 A resolution. Acta Crystallogr D Biol Crystallogr, 51, 380-385. PubMed id: 15299305 DOI: 10.1107/S0907444994011054

Date:

16-Dec-94 Release date: 27-Feb-95

Protein chain

No UniProt id for this chain

Struc: 219 a.a.

Protein chain

No UniProt id for this chain

Struc: 216 a.a.

DOI no: 10.1107/S0907444994011054

Acta Crystallogr D Biol Crystallogr 51:380-385 (1995)

PubMed id: 15299305

Structure of a monoclonal anti-ICAM-1 antibody R6.5 Fab fragment at 2.8 A resolution.

M.J.Jedrzejas, J.Miglietta, J.A.Griffin, M.Luo.

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.

Selected figure(s)

Figure 2.
Fig. 2. A photograph of R6.5 Fab crystals grown in a hanging drop. The rystallization conditions re described in Materials and methods.

Figure 7.
Fig. 7. The surface contour of R6.5 CDRs. The color code for CDRs is, CDRL1, magenta, L2, dark blue, L3, light blue, CDRH1 red, H2, green and H3, yellow. The drawing was made using the RIBBONS program (Caron, 1987).

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1995, 51, 380-385) copyright 1995.

Figures were selected by an automated process.