1zlf
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1zlf |SIZE=350|CAPTION= <scene name='initialview01'>1zlf</scene>, resolution 2.30Å | |PDB= 1zlf |SIZE=350|CAPTION= <scene name='initialview01'>1zlf</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=BOC:TERT-BUTYL+HYDROGEN+CARBONATE'>BOC</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PS0:3(S)-AMINO-4-PHENYL-BUTAN-2(S)-OL'>PS0</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fqx|1FQX]], [[1m0b|1M0B]], [[1lzq|1LZQ]], [[1iiq|1IIQ]], [[1z8c|1Z8C]], [[1zbg|1ZBG]], [[1zj7|1ZJ7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zlf OCA], [http://www.ebi.ac.uk/pdbsum/1zlf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zlf RCSB]</span> | ||
}} | }} | ||
| Line 16: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1ZLF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1ZLF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus Human immunodeficiency virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZLF OCA]. |
==Reference== | ==Reference== | ||
HIV-1 protease mutations and inhibitor modifications monitored on a series of complexes. Structural basis for the effect of the A71V mutation on the active site., Skalova T, Dohnalek J, Duskova J, Petrokova H, Hradilek M, Soucek M, Konvalinka J, Hasek J, J Med Chem. 2006 Sep 21;49(19):5777-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16970402 16970402] | HIV-1 protease mutations and inhibitor modifications monitored on a series of complexes. Structural basis for the effect of the A71V mutation on the active site., Skalova T, Dohnalek J, Duskova J, Petrokova H, Hradilek M, Soucek M, Konvalinka J, Hasek J, J Med Chem. 2006 Sep 21;49(19):5777-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16970402 16970402] | ||
[[Category: HIV-1 retropepsin]] | [[Category: HIV-1 retropepsin]] | ||
| - | [[Category: Human immunodeficiency virus | + | [[Category: Human immunodeficiency virus]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dohnalek, J.]] | [[Category: Dohnalek, J.]] | ||
| Line 28: | Line 31: | ||
[[Category: Petrokova, H.]] | [[Category: Petrokova, H.]] | ||
[[Category: Skalova, T.]] | [[Category: Skalova, T.]] | ||
| - | [[Category: | + | [[Category: hiv]] |
| - | [[Category: | + | [[Category: inhibitor]] |
| + | [[Category: peptidomimetic]] | ||
| + | [[Category: protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:38:18 2008'' |
Revision as of 22:38, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | HIV-1 retropepsin, with EC number 3.4.23.16 | ||||||
| Related: | 1FQX, 1M0B, 1LZQ, 1IIQ, 1Z8C, 1ZBG, 1ZJ7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a complex of mutant HIV-1 protease (A71V, V82T, I84V) with a hydroxyethylamine peptidomimetic inhibitor
Overview
Two new X-ray structures of an HIV-1 protease mutant (A71V, V82T, I84V) in complex with inhibitors SE and SQ, pseudotetrapeptide inhibitors with an acyclic S-hydroxyethylamine isostere, were determined. Comparison of eight structures exploring the binding of four similar inhibitors--SE, SQ (S-hydroxyethylamine isostere), OE (ethyleneamine), and QF34 (hydroxyethylene)--to wild-type and A71V/V82T/I84V HIV-1 protease elucidates the principles of altered interaction with changing conditions. The A71V mutation, which is distant from the active site, causes changes in the structure of the enzyme detectable by the means of X-ray structure analysis, and a route of propagation of the effect toward the active site is proposed.
About this Structure
1ZLF is a Single protein structure of sequence from Human immunodeficiency virus. Full crystallographic information is available from OCA.
Reference
HIV-1 protease mutations and inhibitor modifications monitored on a series of complexes. Structural basis for the effect of the A71V mutation on the active site., Skalova T, Dohnalek J, Duskova J, Petrokova H, Hradilek M, Soucek M, Konvalinka J, Hasek J, J Med Chem. 2006 Sep 21;49(19):5777-84. PMID:16970402
Page seeded by OCA on Mon Mar 31 01:38:18 2008
