From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1bis.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1bis.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1bis| PDB=1bis | SCENE= }} | | {{STRUCTURE_1bis| PDB=1bis | SCENE= }} |
| | | | |
| - | '''HIV-1 INTEGRASE CORE DOMAIN'''
| + | ===HIV-1 INTEGRASE CORE DOMAIN=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | HIV-1 integrase is an essential enzyme in the life cycle of the virus, responsible for catalyzing the insertion of the viral genome into the host cell chromosome; it provides an attractive target for antiviral drug design. The previously reported crystal structure of the HIV-1 integrase core domain revealed that this domain belongs to the superfamily of polynucleotidyltransferases. However, the position of the conserved catalytic carboxylic acids differed from those observed in other enzymes of the class, and attempts to crystallize in the presence of the cofactor, Mg2+, were unsuccessful. We report here three additional crystal structures of the core domain of HIV-1 integrase mutants, crystallized in the presence and absence of cacodylate, as well as complexed with Mg2+. These three crystal forms, containing between them seven independent core domain structures, demonstrate the unambiguous extension of the previously disordered helix alpha4 toward the amino terminus from residue M154 and show that the catalytic E152 points in the general direction of the two catalytic aspartates, D64 and D116. In the vicinity of the active site, the structure of the protein in the absence of cacodylate exhibits significant deviations from the previously reported structures. These differences can be attributed to the modification of C65 and C130 by cacodylate, which was an essential component of the original crystallization mixture. We also demonstrate that in the absence of cacodylate this protein will bind to Mg2+, and could provide a satisfactory platform for binding of inhibitors.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9689049}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9689049 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_9689049}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 34: |
Line 38: |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | [[Category: Integrase]] | | [[Category: Integrase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:34:05 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:13:55 2008'' |
Revision as of 16:13, 30 June 2008
Template:STRUCTURE 1bis
HIV-1 INTEGRASE CORE DOMAIN
Template:ABSTRACT PUBMED 9689049
About this Structure
1BIS is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Three new structures of the core domain of HIV-1 integrase: an active site that binds magnesium., Goldgur Y, Dyda F, Hickman AB, Jenkins TM, Craigie R, Davies DR, Proc Natl Acad Sci U S A. 1998 Aug 4;95(16):9150-4. PMID:9689049
Page seeded by OCA on Mon Jun 30 19:13:55 2008
