1nlb
From Proteopedia
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'''crystal structure of anti-HCV monoclonal antibody 19D9D6''' | '''crystal structure of anti-HCV monoclonal antibody 19D9D6''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLB OCA]. | |
==Reference== | ==Reference== | ||
Crystal structure of a hydrophobic immunodominant antigenic site on hepatitis C virus core protein complexed to monoclonal antibody 19D9D6., Menez R, Bossus M, Muller BH, Sibai G, Dalbon P, Ducancel F, Jolivet-Reynaud C, Stura EA, J Immunol. 2003 Feb 15;170(4):1917-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12574359 12574359] | Crystal structure of a hydrophobic immunodominant antigenic site on hepatitis C virus core protein complexed to monoclonal antibody 19D9D6., Menez R, Bossus M, Muller BH, Sibai G, Dalbon P, Ducancel F, Jolivet-Reynaud C, Stura EA, J Immunol. 2003 Feb 15;170(4):1917-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12574359 12574359] | ||
| - | [[Category: Mus musculus]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Bossus, M.]] | [[Category: Bossus, M.]] | ||
[[Category: Dalbon, P.]] | [[Category: Dalbon, P.]] | ||
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[[Category: Sibai, G.]] | [[Category: Sibai, G.]] | ||
[[Category: Stura, E.]] | [[Category: Stura, E.]] | ||
| - | [[Category: | + | [[Category: Murine monoclonal antibody]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:40:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:40, 2 May 2008
crystal structure of anti-HCV monoclonal antibody 19D9D6
Overview
The first crystal structure of a complex between a hepatitis C virus (HCV) core protein-derived peptide (residues 13-40) and the Ab fragment of a murine mAb (19D9D6) has been solved, allowing determination of the recognized epitope and elucidation of its conformation. This Ab, raised against the first 120 residues of the core protein, recognizes core particles and strongly competes with anticore human Abs, suggesting that it is highly representative of the human anti-HCV core response. Its epitope lies within the first 45 aa of the protein, the major antigenic segment of core recognized both by murine and human Abs. Surprisingly, the recognized epitope (29-37: QIVGGVYLL) has an unusual preponderance of hydrophobic residues, some of which are buried in a small hydrophobic core in the nuclear magnetic resonance structure of the peptide (2-45) in solution, suggesting that the Ab may induce a structural rearrangement upon recognition. The flexibility may reside entirely within the Ag, since the Fab'-peptide complex structure at 2.34 A shows that the Ab binding site is hardly perturbed by complexation. Given that the recognized residues are unlikely to be solvent exposed, we are left with the interesting possibility that Ab-core interactions may take place in a nonaqueous environment.
About this Structure
Full crystallographic information is available from OCA.
Reference
Crystal structure of a hydrophobic immunodominant antigenic site on hepatitis C virus core protein complexed to monoclonal antibody 19D9D6., Menez R, Bossus M, Muller BH, Sibai G, Dalbon P, Ducancel F, Jolivet-Reynaud C, Stura EA, J Immunol. 2003 Feb 15;170(4):1917-24. PMID:12574359 Page seeded by OCA on Sat May 3 02:40:08 2008
