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Structure of Complex of Synthetic HIV-1 Protease with a Substrate-Based Inhibitor at 2.3 Å Resolution

Maria Miller, Jens Schneider, Bangalore K. Sathyanarayana, Mihaly V. Toth, Garland R. Marshall, Leigh Clawson, Linda Selk, Stephen B. H. Kent and Alexander Wlodawer
Science
New Series, Vol. 246, No. 4934 (Dec. 1, 1989), pp. 1149-1152
Stable URL: http://www.jstor.org/stable/1704759
Page Count: 4
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Structure of Complex of Synthetic HIV-1 Protease with a Substrate-Based Inhibitor at 2.3 Å Resolution
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Abstract

The structure of a complex between a peptide inhibitor with the sequence N-acetyl-Thr-Ile-Nle-ψ[CH$_{2}$-NH]-Nle-Gln-Arg.amide (Nle, norleucine) with chemically synthesized HIV-1 (human immunodeficiency virus 1) protease was determined at 2.3 Å 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 Å are observed.

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