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1bai
From Proteopedia
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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]. 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
Page seeded by OCA on Mon Oct 29 20:08:26 2007
Categories: Rous sarcoma virus | Single protein | Adomat, J.M. | Harrison, R.W. | Leis, J. | Louis, J.M. | Ridky, T.W. | Weber, I.T. | Wu, J. | NH2 | Complex (protease/inhibitor) | Crystal structures | Human immunodeficiency virus protease | Protein-mediated interaction | Rous sarcoma virus protease | Viral maturation
