4hvp
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(New page: 200px<br /> <applet load="4hvp" size="450" color="white" frame="true" align="right" spinBox="true" caption="4hvp, resolution 2.3Å" /> '''STRUCTURE OF COMPLEX...)
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Revision as of 12:52, 8 November 2007
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STRUCTURE OF COMPLEX OF SYNTHETIC HIV-1 PROTEASE WITH A STUBTRATE-BASED INHIBITOR AT 2.3 ANGSTROMS RESOLUTION
Overview
The structure of a complex between a peptide inhibitor with the sequence, N-acetyl-Thr-Ile-Nle-psi[CH2-NH]-Nle-Gln-Arg.amide (Nle, norleucine) with, chemically synthesized HIV-1 (human immunodeficiency virus 1) protease was, determined at 2.3 A resolution (R factor of 0.176). Despite the symmetric, nature of the unliganded enzyme, the asymmetric inhibitor lies in a single, orientation and makes extensive interactions at the interface between the, two subunits of the homodimeric protein. Compared with the unliganded, enzyme, the protein molecule underwent substantial changes, particularly, in an extended region corresponding to the "flaps" (residues 35 to 57 in, each chain), where backbone movements as large as 7 A are observed.
About this Structure
4HVP is a Single protein structure of sequence from Human immunodeficiency virus 1 with ACE and NH2 as ligands. Full crystallographic information is available from OCA.
Reference
Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution., Miller M, Schneider J, Sathyanarayana BK, Toth MV, Marshall GR, Clawson L, Selk L, Kent SB, Wlodawer A, Science. 1989 Dec 1;246(4934):1149-52. PMID:2686029
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