Solution conformation and dynamics of the HIV-1 integrase core domain
NC Fitzkee, JE Masse, Y Shen, DR Davies… - Journal of Biological …, 2010 - ASBMB
The human immunodeficiency virus type 1 (HIV-1) integrase (IN) is a critical enzyme
involved in infection. It catalyzes two reactions to integrate the viral cDNA into the host …
involved in infection. It catalyzes two reactions to integrate the viral cDNA into the host …
The Mobility of an HIV-1 Integrase Active Site Loop Is Correlated with Catalytic Activity,
J Greenwald, V Le, SL Butler, FD Bushman… - Biochemistry, 1999 - ACS Publications
Replication of HIV-1 requires the covalent integration of the viral cDNA into the host
chromosomal DNA directed by the virus-encoded integrase protein. Here we explore the …
chromosomal DNA directed by the virus-encoded integrase protein. Here we explore the …
Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding
JCH Chen, J Krucinski, LJW Miercke… - Proceedings of the …, 2000 - National Acad Sciences
Insolubility of full-length HIV-1 integrase (IN) limited previous structure analyses to individual
domains. By introducing five point mutations, we engineered a more soluble IN that allowed …
domains. By introducing five point mutations, we engineered a more soluble IN that allowed …
[HTML][HTML] Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding site
HIV integrase (IN) is an essential enzyme in HIV replication and an important target for drug
design. IN has been shown to interact with a number of cellular and viral proteins during the …
design. IN has been shown to interact with a number of cellular and viral proteins during the …
[HTML][HTML] Four-tiered π interaction at the dimeric interface of HIV-1 integrase critical for DNA integration and viral infectivity
HIV-1 integrase (IN) is an essential enzyme for viral infection. Here, we report an extensive π
electron orbital interaction between four amino acids, W132, M178, F181 and F185, located …
electron orbital interaction between four amino acids, W132, M178, F181 and F185, located …
Three new structures of the core domain of HIV-1 integrase: an active site that binds magnesium
Y Goldgur, F Dyda, AB Hickman… - Proceedings of the …, 1998 - National Acad Sciences
HIV-1 integrase is an essential enzyme in the life cycle of the virus, responsible for
catalyzing the insertion of the viral genome into the host cell chromosome; it provides an …
catalyzing the insertion of the viral genome into the host cell chromosome; it provides an …
Subunit-specific protein footprinting reveals significant structural rearrangements and a role for N-terminal Lys-14 of HIV-1 Integrase during viral DNA binding
Z Zhao, CJ McKee, JJ Kessl, WL Santos… - Journal of Biological …, 2008 - ASBMB
To identify functional contacts between HIV-1 integrase (IN) and its viral DNA substrate, we
devised a new experimental strategy combining the following two methodologies. First …
devised a new experimental strategy combining the following two methodologies. First …
The solution structure of the amino-terminal HHCC domain of HIV-2 integrase: a three-helix bundle stabilized by zinc
APAM Eijkelenboom, FMI van den Ent, A Vos… - Current Biology, 1997 - cell.com
Background: Integrase mediates a crucial step in the life cycle of the human
immunodeficiency virus (HIV). The enzyme cleaves the viral DNA ends in a sequence …
immunodeficiency virus (HIV). The enzyme cleaves the viral DNA ends in a sequence …
[HTML][HTML] Single amino acid substitution in HIV-1 integrase catalytic core causes a dramatic shift in inhibitor selectivity
LQ Al-Mawsawi, M Sechi, N Neamati - FEBS letters, 2007 - Elsevier
HIV-1 integrase (IN) mediates the insertion of viral cDNA into the cell genome, a vital
process for replication. This step is catalyzed by two separate DNA reaction events, termed …
process for replication. This step is catalyzed by two separate DNA reaction events, termed …
A metal-induced conformational change and activation of HIV-1 integrase
E Asante-Appiah, AM Skalka - Journal of Biological Chemistry, 1997 - ASBMB
Retroviral integrases are composed of three independently folding domains whose
organization relevant to one another is largely unknown. As an approach to understanding …
organization relevant to one another is largely unknown. As an approach to understanding …