Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity.
Zheng, R
Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America Nov 1996 - 13659-64 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0027-8424
10.1073/pnas.93.24.13659 doi
Amino Acid Sequence
Apoenzymes--chemistry
Catalysis
Circular Dichroism
Conserved Sequence
Cystine
DNA, Viral--chemistry
HIV Integrase--chemistry
HIV-1--enzymology
Kinetics
Macromolecular Substances
Mutagenesis, Site-Directed
Oligodeoxyribonucleotides--chemistry
Point Mutation
Protein Conformation
Protein Folding
Recombinant Proteins--chemistry
Spectrophotometry, Atomic
Substrate Specificity
Zinc--analysis
Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America Nov 1996 - 13659-64 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0027-8424
10.1073/pnas.93.24.13659 doi
Amino Acid Sequence
Apoenzymes--chemistry
Catalysis
Circular Dichroism
Conserved Sequence
Cystine
DNA, Viral--chemistry
HIV Integrase--chemistry
HIV-1--enzymology
Kinetics
Macromolecular Substances
Mutagenesis, Site-Directed
Oligodeoxyribonucleotides--chemistry
Point Mutation
Protein Conformation
Protein Folding
Recombinant Proteins--chemistry
Spectrophotometry, Atomic
Substrate Specificity
Zinc--analysis