1WJA

SOLUTION STRUCTURE OF THE N-TERMINAL ZN BINDING DOMAIN OF HIV-1 INTEGRASE (D FORM), NMR, REGULARIZED MEAN STRUCTURE

Summary for 1WJA

• Entry DOI: 10.2210/pdb1wja/pdb
• Descriptor: HIV-1 INTEGRASE, ZINC ION (2 entities in total)
• Functional Keywords: zn-binding protein, aids, polyprotein, hydrolase, aspartyl protease, endonuclease
• Biological source: Human immunodeficiency virus 1
• Cellular location: Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P35963
• Total number of polymer chains: 2
• Total formula weight: 10786.86

Authors

Clore, G.M.,Cai, M.,Caffrey, M.,Gronenborn, A.M. (deposition date: 1997-05-13, release date: 1998-05-13, Last modification date: 2024-05-22)

Primary citation

Cai, M.,Zheng, R.,Caffrey, M.,Craigie, R.,Clore, G.M.,Gronenborn, A.M.
Solution structure of the N-terminal zinc binding domain of HIV-1 integrase.
Nat.Struct.Biol., 4:567-577, 1997

PubMed Abstract: The solution structure of the N-terminal zinc binding domain (residues 1-55; IN1-55) of HIV-1 integrase has been solved by NMR spectroscopy. IN1-55 is dimeric, and each monomer comprises four helices with the zinc tetrahedrally coordinated to His 12, His 16, Cys 40 and Cys 43. IN1-55 exists in two interconverting conformational states that differ with regard to the coordination of the two histidine side chains to zinc. The different histidine arrangements are associated with large conformational differences in the polypeptide backbone (residues 9-18) around the coordinating histidines. The dimer interface is predominantly hydrophobic and is formed by the packing of the N-terminal end of helix 1, and helices 3 and 4. The monomer fold is remarkably similar to that of a number of helical DNA binding proteins containing a helix-turn-helix (HTH) motif with helices 2 and 3 of IN1-55 corresponding to the HTH motif. In contrast to the DNA binding proteins where the second helix of the HTH motif is employed for DNA recognition, IN1-55 uses this helix for dimerization.

PubMed: 9228950
DOI: 10.1038/nsb0797-567

Experimental method

SOLUTION NMR