1ivq
From Proteopedia
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|PDB= 1ivq |SIZE=350|CAPTION= <scene name='initialview01'>1ivq</scene>, resolution 2.6Å | |PDB= 1ivq |SIZE=350|CAPTION= <scene name='initialview01'>1ivq</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=CPV:5-AMINO-6-CYCLOHEXYL-4-HYDROXY-2-ISOPROPYL-HEXANOIC+ACID'>CPV</scene>, <scene name='pdbligand=NPT:NEOPENTYLAMINE'>NPT</scene>, <scene name='pdbligand=QNC:2-CARBONYLQUINOLINE'>QNC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ivq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivq OCA], [http://www.ebi.ac.uk/pdbsum/1ivq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ivq RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IVQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1IVQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_2 Human immunodeficiency virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVQ OCA]. |
==Reference== | ==Reference== | ||
The crystallographic structure of the protease from human immunodeficiency virus type 2 with two synthetic peptidic transition state analog inhibitors., Mulichak AM, Hui JO, Tomasselli AG, Heinrikson RL, Curry KA, Tomich CS, Thaisrivongs S, Sawyer TK, Watenpaugh KD, J Biol Chem. 1993 Jun 25;268(18):13103-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8514751 8514751] | The crystallographic structure of the protease from human immunodeficiency virus type 2 with two synthetic peptidic transition state analog inhibitors., Mulichak AM, Hui JO, Tomasselli AG, Heinrikson RL, Curry KA, Tomich CS, Thaisrivongs S, Sawyer TK, Watenpaugh KD, J Biol Chem. 1993 Jun 25;268(18):13103-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8514751 8514751] | ||
| - | [[Category: Human immunodeficiency virus | + | [[Category: Human immunodeficiency virus 2]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Mulichak, A M.]] | [[Category: Mulichak, A M.]] | ||
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[[Category: hydrolase(acid proteinase)]] | [[Category: hydrolase(acid proteinase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:25:17 2008'' |
Revision as of 18:25, 30 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTALLOGRAPHIC STRUCTURE OF THE PROTEASE FROM HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 WITH TWO SYNTHETIC PEPTIDIC TRANSITION STATE ANALOG INHIBITORS
Overview
The crystal structure of human immunodeficiency virus (HIV) type 2 protease has been determined in complexes with peptidic inhibitors Noa-His-Cha psi [CH(OH)CH(OH)]Val-Ile-Amp (U75875) and Qnc-Asn-Cha psi [CH(OH)CH2]Val-Npt(U92163) (where Noa is naphthyloxyacetyl, Cha is cyclohexylalanine, Amp is 2-aminomethylpyridine, Qnc is quinoline-2-carbonyl, and Npt is neopentylamine), which have dihydroxyethylene and hydroxyethylene moieties, respectively, in place of the normal scissile bond of the natural ligand. The complexes crystallize in space group P2(1)2(1)2(1), with one dimer-inhibitor complex per asymmetric unit and average cell dimensions of a = 33.28 A, b = 45.35 A, c = 135.84 A. Data were collected to approximately 2.5-A resolution. The model structures were refined with resulting R-factors of around 0.19. As expected, the HIV-2 protease structure is approximately C2-symmetric with a gross structure very similar to that of the HIV-1 enzyme. The inhibitors bind in an extended conformation positioned lengthwise in the binding cleft in a manner similar to that found in the HIV-1 protease-inhibitor complexes previously reported. The substitution of the bulkier Ile82 side chain in the HIV-2 protease may help explain the better ability of HIV-2 protease to bind and hydrolyze ligands with small P1 and P1' side groups. It appears that differences in specificity between the proteases of HIV-1 and HIV-2 are not merely a result of simple side chain substitutions, but may be complicated by differences in main chain flexibility as well.
About this Structure
1IVQ is a Single protein structure of sequence from Human immunodeficiency virus 2. Full crystallographic information is available from OCA.
Reference
The crystallographic structure of the protease from human immunodeficiency virus type 2 with two synthetic peptidic transition state analog inhibitors., Mulichak AM, Hui JO, Tomasselli AG, Heinrikson RL, Curry KA, Tomich CS, Thaisrivongs S, Sawyer TK, Watenpaugh KD, J Biol Chem. 1993 Jun 25;268(18):13103-9. PMID:8514751
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