PDBsum entry 2v7h

Immune system

PDB id: 2v7h

Contents

Protein chains

214 a.a. *

216 a.a. *

Waters ×106

* Residue conservation analysis

PDB id:

2v7h

Name:

Immune system

Title:

Crystal structure of an immunogen specific anti-mannopyranoside monoclonal antibody fab fragment

Structure:

Monoclonal antibody. Chain: a, l. Fragment: fab fragment light chain. Other_details: monoclonal antibody against alpha-d-mannopyranoside. Monoclonal antibody. Chain: b, h. Fragment: fab fragment heavy chain. Other_details: monoclonal antibody against alpha-d-mannopyranoside

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Strain: balb/c. Cell_line: 1h7 murine hybridoma. Cell: b-lymphocyte. Cell: b-lymphocyte

Resolution:

2.80Å R-factor: 0.242 R-free: 0.268

Authors:

L.Krishnan,G.Sahni,K.J.Kaur,D.M.Salunke

Key ref:

L.Krishnan et al. (2008). Role of antibody paratope conformational flexibility in the manifestation of molecular mimicry. Biophys J, 94, 1367-1376. PubMed id: 18032557

Date:

30-Jul-07 Release date: 19-Aug-08

Protein chains

No UniProt id for this chain

Struc: 214 a.a.

Protein chains

No UniProt id for this chain

Struc: 216 a.a.

Biophys J 94:1367-1376 (2008)

PubMed id: 18032557

Role of antibody paratope conformational flexibility in the manifestation of molecular mimicry.

L.Krishnan, G.Sahni, K.J.Kaur, D.M.Salunke.

ABSTRACT

Molecular mimicry is a recurrent theme in host defense processes. The correlation of functional mimicry with the structural features of the antibody paratope has been investigated, addressing the consequences of mimicry in host immune mechanisms. Two anti-mannopyranoside antibodies, 1H7 and 2D10, representing the possible extremes of the recognition spectrum with regard to peptide-carbohydrate mimicry were examined. Crystallographic and molecular dynamics simulation analyses established correlation between the antibody flexibility and the manifestation of mimicry. It was evident that monoclonal antibody (mAb) 1H7, which has a narrow specificity in favor of the immunizing antigen, exhibited structural invariance. On the other hand, the antigen-combining site of 2D10, the mimicry-recognizing antibody, showed substantial divergence in the complementarity determining region loops. The docking of mannopyranoside within the antibody paratope revealed multiple modes of binding of the carbohydrate antigen in mAb 2D10 vis à vis single docking mode in mAb 1H7, which overlapped with the common monosaccharide binding site defined in anti-carbohydrate antibodies. The presence of additional antigen binding modes is perhaps reflective of the utilization of conformational flexibility in molecular mimicry. A relatively broader recognition repertoire--attributable to paratope flexibility--may facilitate the recognition of altered antigens of invading pathogens while the antibodies with narrow recognition specificity maintain the fidelity of the response.