1JP5

Crystal structure of the single-chain Fv fragment 1696 in complex with the epitope peptide corresponding to N-terminus of HIV-1 protease

Summary for 1JP5

• Entry DOI: 10.2210/pdb1jp5/pdb
• Related: 1CL7 1MF2 2HRP
• Descriptor: single-chain Fv fragment 1696, epitope peptide corresponding to N-terminus of HIV-1 protease (3 entities in total)
• Functional Keywords: antibody-antigen complex, hiv pr inhibiting antibody, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 4
• Total formula weight: 56152.11

Authors

Rezacova, P.,Lescar, J.,Brynda, J.,Fabry, M.,Horejsi, M.,Sedlacek, J.,Bentley, G.A. (deposition date: 2001-08-01, release date: 2001-10-12, Last modification date: 2024-11-13)

Primary citation

Rezacova, P.,Lescar, J.,Brynda, J.,Fabry, M.,Horejsi, M.,Sedlacek, J.,Bentley, G.A.
Structural basis of HIV-1 and HIV-2 protease inhibition by a monoclonal antibody.
Structure, 9:887-895, 2001

PubMed Abstract: Since the demonstration that the protease of the human immunodeficiency virus (HIV Pr) is essential in the viral life cycle, this enzyme has become one of the primary targets for antiviral drug design. The murine monoclonal antibody 1696 (mAb1696), produced by immunization with the HIV-1 protease, inhibits the catalytic activity of the enzyme of both the HIV-1 and HIV-2 isolates with inhibition constants in the low nanomolar range. The antibody cross-reacts with peptides that include the N terminus of the enzyme, a region that is highly conserved in sequence among different viral strains and that, furthermore, is crucial for homodimerization to the active enzymatic form.

PubMed: 11591344
DOI: 10.1016/S0969-2126(01)00654-2

Experimental method

X-RAY DIFFRACTION (2.7 Å)