1995
DOI: 10.1021/bi00031a002
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Solution Structure of the DNA Binding Domain of HIV-1 Integrase

Abstract: The solution structure of the DNA binding domain of HIV-1 integrase (residues 220-270) has been determined by multidimensional NMR spectroscopy. The protein is a dimer in solution, and each subunit is composed of a five-stranded beta-barrel with a topology very similar to that of the SH3 domain. The dimer is formed by a stacked beta-interface comprising strands 2, 3, and 4, with the two triple-stranded antiparallel beta-sheets, one from each subunit, oriented antiparallel to each other. One surface of the dime… Show more

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Cited by 295 publications
(306 citation statements)
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“…The NMR structure for residues 220-270 of the HIV-1 C-terminal domain is a dimer involving antiparallel, 2-fold related packing of the contiguous ␤2-␤3-␤4 three-stranded ␤-sheets against each other (16,17). Although it differs from all three C-terminal interfaces in the IN 52-288 crystal structure, the NMR dimer interface most closely resembles IN 52-288 interface B that involves the ␤2-␤3-␤4 sheets.…”
Section: Discussionmentioning
confidence: 96%
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“…The NMR structure for residues 220-270 of the HIV-1 C-terminal domain is a dimer involving antiparallel, 2-fold related packing of the contiguous ␤2-␤3-␤4 three-stranded ␤-sheets against each other (16,17). Although it differs from all three C-terminal interfaces in the IN 52-288 crystal structure, the NMR dimer interface most closely resembles IN 52-288 interface B that involves the ␤2-␤3-␤4 sheets.…”
Section: Discussionmentioning
confidence: 96%
“…The mutation F185K markedly improved solubility of the central IN catalytic core domain to over 25 mg͞ml and led to its crystal structure (12,13). Structures of the individual N-terminal (14,15) and C-terminal domains (16)(17)(18) have been determined by NMR. Like the catalytic core domain, each isolated terminal domain dimerizes in solution.…”
mentioning
confidence: 99%
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“…SH3-like folds are not only found in intracellular proteins of eukaryotes but also in extracellular proteins like MIA (Stoll et al, 2001), in virus genes and even in prokaryotes (Whisstock and Lesk, 1999). The DNAbinding domain of the HIV-1 integrase has an SH3-like structure (Eijkelenboom et al, 1995;Lodi et al, 1995). The same is true for the metal binding domain of the cobalt-activated diphtheria toxin repressor-DNA complex (Pohl et al, 1999).…”
Section: Sh3mentioning
confidence: 99%
“…Crystallographic or NMR structural data are available for each of the individual domains (11)(12)(13)(14)(15). In addition, two-domain crystal structures [either the core and C-terminal domains (16), or N-terminal and the core domains (17) of HIV-1 IN] have been recently determined.…”
mentioning
confidence: 99%