1bai

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spinqualitylabelsall models 1bai, resolution 2.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURAL BASIS FOR SPECIFICITY OF RETROVIRAL PROTEASES

Overview

The Rous sarcoma virus (RSV) protease S9 variant has been engineered to, exhibit high affinity for HIV-1 protease substrates and inhibitors in, order to verify the residues deduced to be critical for the specificity, differences. The variant has 9 substitutions (S38T, I42D, I44V, M73V, A100L, V104T, R105P, G106V, and S107N) of structurally equivalent residues, from HIV-1 protease. Unlike the wild-type enzyme, RSV S9 protease, hydrolyzes peptides representing the HIV-1 protease polyprotein cleavage, sites. The crystal structure of RSV S9 protease with the inhibitor, Arg-Val-Leu-r-Phe-Glu-Ala-Nle-NH2, a reduced peptide analogue of the HIV-1, CA-p2 cleavage site, has been refined to an R factor of 0.175 at 2.4-A, resolution. The structure shows flap residues that were not visible in the, ... [(full description)]

About this Structure

1BAI is a [Single protein] structure of sequence from [Rous sarcoma virus] with NH2 as [ligand]. Structure known Active Site: NUL. Full crystallographic information is available from [OCA].

Reference

Structural basis for specificity of retroviral proteases., Wu J, Adomat JM, Ridky TW, Louis JM, Leis J, Harrison RW, Weber IT, Biochemistry. 1998 Mar 31;37(13):4518-26. PMID:9521772

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