1SVZ

Crystal structure of the single-chain Fv fragment 1696 in complex with the epitope peptide corresponding to N-terminus of HIV-2 protease

Summary for 1SVZ

• Entry DOI: 10.2210/pdb1svz/pdb
• Related: 1Cl2 1JP5 1MF2 1N4X 2HRP
• Descriptor: single-chain Fv fragment 1696, epitope peptide corresponding to N-terminus of HIV-2 protease (3 entities in total)
• Functional Keywords: antibody-antigen complex; hiv inhibiting antibody, immune system
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 4
• Total formula weight: 55879.80

Authors

Rezacova, P.,Brynda, J.,Lescar, J.,Bentley, G.A.,Fabry, M.,Horejsi, M.,Sedlacek, J. (deposition date: 2004-03-30, release date: 2005-03-01, Last modification date: 2024-10-30)

Primary citation

Rezacova, P.,Brynda, J.,Lescar, J.,Fabry, M.,Horejsi, M.,Sieglova, I.,Sedlacek, J.,Bentley, G.A.
Crystal structure of a cross-reaction complex between an anti-HIV-1 protease antibody and an HIV-2 protease peptide
J.Struct.Biol., 149:332-337, 2005

PubMed Abstract: The monoclonal antibody 1696, elicited by HIV-1 protease, inhibits the activity of both HIV-1 and HIV-2 proteases with inhibition constants in the low nanomolar range. The antibody cross-reacts with peptides derived from the N-terminal region of both proteases. The crystal structure of the recombinant single-chain Fv fragment of 1696 complexed with an N-terminal peptide from the HIV-2 protease has been determined at 1.88A resolution. Interactions of the peptide with scFv1696 are compared with the previously reported structure of scFv1696 in complex with the corresponding peptide from HIV-1 protease. The origin of cross-reactivity of mAb1696 with HIV proteases is discussed.

PubMed: 15721587
DOI: 10.1016/j.jsb.2004.11.009

Experimental method

X-RAY DIFFRACTION (1.89 Å)