1WJF

SOLUTION STRUCTURE OF H12C MUTANT OF THE N-TERMINAL ZN BINDING DOMAIN OF HIV-1 INTEGRASE COMPLEXED TO CADMIUM, NMR, 40 STRUCTURES

Summary for 1WJF

• Entry DOI: 10.2210/pdb1wjf/pdb
• Descriptor: HIV-1 INTEGRASE, CADMIUM ION (2 entities in total)
• Functional Keywords: zn-binding protein, aids, polyprotein, hydrolase, aspartyl protease
• Biological source: Human immunodeficiency virus 1
• Cellular location: Gag-Pol polyprotein: Host cell membrane; Lipid-anchor. Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P04587
• Total number of polymer chains: 2
• Total formula weight: 12548.72

Authors

Cai, M.,Gronenborn, A.M.,Clore, G.M. (deposition date: 1998-06-11, release date: 1998-12-16, Last modification date: 2024-05-01)

Primary citation

Cai, M.,Huang, Y.,Caffrey, M.,Zheng, R.,Craigie, R.,Clore, G.M.,Gronenborn, A.M.
Solution structure of the His12 --> Cys mutant of the N-terminal zinc binding domain of HIV-1 integrase complexed to cadmium.
Protein Sci., 7:2669-2674, 1998

PubMed Abstract: The solution structure of His12 --> Cys mutant of the N-terminal zinc binding domain (residues 1-55; IN(1-55)) of HIV-1 integrase complexed to cadmium has been solved by multidimensional heteronuclear NMR spectroscopy. The overall structure is very similar to that of the wild-type N-terminal domain complexed to zinc. In contrast to the wild-type domain, however, which exists in two interconverting conformational states arising from different modes of coordination of the two histidine side chains to the metal, the cadmium complex of the His12 --> Cys mutant exists in only a single form at low pH. The conformation of the polypeptide chain encompassing residues 10-18 is intermediate between the two forms of the wild-type complex.

PubMed: 9865962

Experimental method

SOLUTION NMR