Insights from Atomic-Resolution X-Ray Structures of Chemically Synthesized HIV-1 Protease in Complex with Inhibitors.

Erik C.B. Johnson; Enrico Malito; Yuequan Shen; Brad Pentelute; Dan Rich; Jan Florián; Wei-Jen Tang; Stephen B.H. Kent; Jan Florian

doi:10.1016/j.jmb.2007.07.054

Insights from Atomic-Resolution X-Ray Structures of Chemically Synthesized HIV-1 Protease in Complex with Inhibitors.

Erik C.B. Johnson
, Enrico Malito
, Yuequan Shen
, Brad Pentelute
, Dan Rich
, Jan Florián
, Wei-Jen Tang
, Stephen B.H. Kent
, Jan Florian

University of Chicago
University of Wisconsin-Madison
Loyola University Chicago

Research output: Contribution to journal › Article › peer-review

Original language	American English
Journal	Journal of Molecular Biology
Volume	373
Issue number	3
DOIs	https://doi.org/10.1016/j.jmb.2007.07.054
State	Published - Jan 10 2007

Disciplines

Biochemistry

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@article{87085586bae045c7b0cf6c31ffbd929a,

title = "Insights from Atomic-Resolution X-Ray Structures of Chemically Synthesized HIV-1 Protease in Complex with Inhibitors.",

author = "Johnson, \{Erik C.B.\} and Enrico Malito and Yuequan Shen and Brad Pentelute and Dan Rich and Jan Flori{\'a}n and Wei-Jen Tang and Kent, \{Stephen B.H.\} and Jan Florian",

note = "The human immunodeficiency virus 1 (HIV-1) protease (PR) is an aspartyl protease essential for HIV-1 viral infectivity. HIV-1 PR has one catalytic site formed by the homodimeric enzyme. We chemically synthesized fully active HIV-1 PR using modern ligation methods.",

year = "2007",

month = jan,

day = "10",

doi = "10.1016/j.jmb.2007.07.054",

language = "American English",

volume = "373",

journal = "Journal of Molecular Biology",

number = "3",

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TY - JOUR

T1 - Insights from Atomic-Resolution X-Ray Structures of Chemically Synthesized HIV-1 Protease in Complex with Inhibitors.

AU - Johnson, Erik C.B.

AU - Malito, Enrico

AU - Shen, Yuequan

AU - Pentelute, Brad

AU - Rich, Dan

AU - Florián, Jan

AU - Tang, Wei-Jen

AU - Kent, Stephen B.H.

AU - Florian, Jan

N1 - The human immunodeficiency virus 1 (HIV-1) protease (PR) is an aspartyl protease essential for HIV-1 viral infectivity. HIV-1 PR has one catalytic site formed by the homodimeric enzyme. We chemically synthesized fully active HIV-1 PR using modern ligation methods.

PY - 2007/1/10

Y1 - 2007/1/10

UR - https://www.sciencedirect.com/science/article/pii/S0022283607010078

U2 - 10.1016/j.jmb.2007.07.054

DO - 10.1016/j.jmb.2007.07.054

M3 - Article

VL - 373

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 3

ER -

Insights from Atomic-Resolution X-Ray Structures of Chemically Synthesized HIV-1 Protease in Complex with Inhibitors.

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