1az5
From Proteopedia
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(New page: 200px<br /> <applet load="1az5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1az5, resolution 2.0Å" /> '''UNLIGANDED SIV PROTE...)
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Revision as of 19:27, 29 October 2007
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UNLIGANDED SIV PROTEASE STRUCTURE IN AN "OPEN" CONFORMATION
Overview
Rigid body rotation of five domains and movements within their interfacial, joints provide a rational context for understanding why HIV protease, mutations that arise in drug resistant strains are often spatially removed, from the drug or substrate binding sites. Domain motions associated with, substrate binding in the retroviral HIV-1 and SIV proteases are identified, and characterized. These motions are in addition to closure of the flaps, and result from rotations of approximately 6-7 degrees at primarily, hydrophobic interfaces. A crystal structure of unliganded SIV protease, (incorporating the point mutation Ser 4 His to stabilize the protease, against autolysis) was determined to 2.0 A resolution in a new space, group, P3221. The structure is in the most "open" conformation of any, ... [(full description)]
About this Structure
1AZ5 is a [Single protein] structure of sequence from [Chimpanzee immunodeficiency virus]. Active as [[1]], with EC number [3.4.23.16]. Full crystallographic information is available from [OCA].
Reference
Domain flexibility in retroviral proteases: structural implications for drug resistant mutations., Rose RB, Craik CS, Stroud RM, Biochemistry. 1998 Feb 24;37(8):2607-21. PMID:9485411
Page seeded by OCA on Mon Oct 29 21:32:22 2007
