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1axa
From Proteopedia
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===ACTIVE-SITE MOBILITY IN HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 PROTEASE AS DEMONSTRATED BY CRYSTAL STRUCTURE OF A28S MUTANT=== | ===ACTIVE-SITE MOBILITY IN HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 PROTEASE AS DEMONSTRATED BY CRYSTAL STRUCTURE OF A28S MUTANT=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1axa]] is a 2 chain structure of [[Virus protease]] with sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AXA OCA]. | |
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| + | ==See Also== | ||
| + | *[[Virus protease|Virus protease]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:009521105</ref><ref group="xtra">PMID:019105629</ref><references group="xtra"/> |
[[Category: HIV-1 retropepsin]] | [[Category: HIV-1 retropepsin]] | ||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
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[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Mutant]] | [[Category: Mutant]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 23:15:49 2009'' | ||
Revision as of 01:56, 26 July 2012
Contents |
ACTIVE-SITE MOBILITY IN HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 PROTEASE AS DEMONSTRATED BY CRYSTAL STRUCTURE OF A28S MUTANT
Template:ABSTRACT PUBMED 9521105
About this Structure
1axa is a 2 chain structure of Virus protease with sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
See Also
Reference
- Hong L, Hartsuck JA, Foundling S, Ermolieff J, Tang J. Active-site mobility in human immunodeficiency virus, type 1, protease as demonstrated by crystal structure of A28S mutant. Protein Sci. 1998 Feb;7(2):300-5. PMID:9521105
- Bannwarth L, Rose T, Dufau L, Vanderesse R, Dumond J, Jamart-Gregoire B, Pannecouque C, De Clercq E, Reboud-Ravaux M. Dimer disruption and monomer sequestration by alkyl tripeptides are successful strategies for inhibiting wild-type and multidrug-resistant mutated HIV-1 proteases. Biochemistry. 2009 Jan 20;48(2):379-87. PMID:19105629 doi:10.1021/bi801422u
