2nxm
From Proteopedia
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===Structure of HIV-1 protease D25N complexed with the rt-rh analogue peptide GLY-ALA-GLN-THR-PHE*TYR-VAL-ASP-GLY-ALA=== | ===Structure of HIV-1 protease D25N complexed with the rt-rh analogue peptide GLY-ALA-GLN-THR-PHE*TYR-VAL-ASP-GLY-ALA=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[2nxm]] is a 3 chain structure of [[Virus protease]] with sequence from [http://en.wikipedia.org/wiki/Hiv-1_m:b_arv2/sf2 Hiv-1 m:b_arv2/sf2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NXM OCA]. | |
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| + | ==See Also== | ||
| + | *[[Virus protease|Virus protease]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:017729291</ref><references group="xtra"/> |
[[Category: HIV-1 retropepsin]] | [[Category: HIV-1 retropepsin]] | ||
| - | [[Category: | + | [[Category: Hiv-1 m:b_arv2/sf2]] |
[[Category: Nalivaika, E.]] | [[Category: Nalivaika, E.]] | ||
[[Category: Prabu-Jeyabalan, M.]] | [[Category: Prabu-Jeyabalan, M.]] | ||
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[[Category: Calorimetry]] | [[Category: Calorimetry]] | ||
[[Category: Hiv protease]] | [[Category: Hiv protease]] | ||
| - | [[Category: Hydrolase | + | [[Category: Hydrolase-hydrolase substrate complex]] |
[[Category: Molecular dynamic]] | [[Category: Molecular dynamic]] | ||
[[Category: Peptide design]] | [[Category: Peptide design]] | ||
[[Category: Substrate recognition]] | [[Category: Substrate recognition]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 20:17:24 2009'' | ||
Revision as of 22:50, 25 July 2012
Contents |
Structure of HIV-1 protease D25N complexed with the rt-rh analogue peptide GLY-ALA-GLN-THR-PHE*TYR-VAL-ASP-GLY-ALA
Template:ABSTRACT PUBMED 17729291
About this Structure
2nxm is a 3 chain structure of Virus protease with sequence from Hiv-1 m:b_arv2/sf2. Full crystallographic information is available from OCA.
See Also
Reference
- Altman MD, Nalivaika EA, Prabu-Jeyabalan M, Schiffer CA, Tidor B. Computational design and experimental study of tighter binding peptides to an inactivated mutant of HIV-1 protease. Proteins. 2008 Feb 15;70(3):678-94. PMID:17729291 doi:10.1002/prot.21514
