1har: Difference between revisions
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[[Image:1har.gif|left|200px]] | [[Image:1har.gif|left|200px]] | ||
'''2.2 ANGSTROMS RESOLUTION STRUCTURE OF THE AMINO-TERMINAL HALF OF HIV-1 REVERSE TRANSCRIPTASE (FINGERS AND PALM SUBDOMAINS)''' | {{Structure | ||
|PDB= 1har |SIZE=350|CAPTION= <scene name='initialview01'>1har</scene>, resolution 2.2Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] | |||
|GENE= | |||
}} | |||
'''2.2 ANGSTROMS RESOLUTION STRUCTURE OF THE AMINO-TERMINAL HALF OF HIV-1 REVERSE TRANSCRIPTASE (FINGERS AND PALM SUBDOMAINS)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HAR is a [ | 1HAR is a [[Single protein]] structure of 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=1HAR OCA]. | ||
==Reference== | ==Reference== | ||
2.2 A resolution structure of the amino-terminal half of HIV-1 reverse transcriptase (fingers and palm subdomains)., Unge T, Knight S, Bhikhabhai R, Lovgren S, Dauter Z, Wilson K, Strandberg B, Structure. 1994 Oct 15;2(10):953-61. PMID:[http:// | 2.2 A resolution structure of the amino-terminal half of HIV-1 reverse transcriptase (fingers and palm subdomains)., Unge T, Knight S, Bhikhabhai R, Lovgren S, Dauter Z, Wilson K, Strandberg B, Structure. 1994 Oct 15;2(10):953-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7532533 7532533] | ||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
[[Category: RNA-directed DNA polymerase]] | [[Category: RNA-directed DNA polymerase]] | ||
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[[Category: reverse transcriptase]] | [[Category: reverse transcriptase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:34:41 2008'' | ||
Revision as of 12:34, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Activity: | RNA-directed DNA polymerase, with EC number 2.7.7.49 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
2.2 ANGSTROMS RESOLUTION STRUCTURE OF THE AMINO-TERMINAL HALF OF HIV-1 REVERSE TRANSCRIPTASE (FINGERS AND PALM SUBDOMAINS)
OverviewOverview
BACKGROUND: HIV-1 reverse transcriptase (RT) catalyzes the transformation of single-stranded viral RNA into double-stranded DNA, which is integrated into host cell chromosomes. The molecule is a heterodimer of two subunits, p51 and p66. The amino acid sequence of p51 is identical to the sequence of the amino-terminal subdomains of p66. Earlier crystallographic studies indicate that the RT molecule is flexible, which may explain the difficulty in obtaining high-resolution data for the intact protein. We have therefore determined the structure of a fragment of RT (RT216), which contains only the amino-terminal half of the RT molecule ('finger' and 'palm' subdomains). RESULTS: The crystal structure of RT216 has been refined at 2.2 A resolution to a crystallographic R-value of 20.8%. The structure is very similar to that of the corresponding part of the p66 subunit in the p66/p51 heterodimer, although there is a small difference in the relative orientation of the two subdomains compared with the structure of an RT-DNA-antibody fragment complex. There are a large number of stabilizing contacts (mainly hydrogen bonds and hydrophobic interactions) between the subdomains. The locations of conserved amino acids and the position of some important drug-resistant mutations are described. CONCLUSIONS: The RT216 structure provides detailed three-dimensional information of one important part of HIV-1 RT (including the critical active site residues). We propose a model to explain the inhibitory effect of non-nucleoside inhibitors, which partially accounts for their effect in terms of conformational changes of active site residues.
About this StructureAbout this Structure
1HAR is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
ReferenceReference
2.2 A resolution structure of the amino-terminal half of HIV-1 reverse transcriptase (fingers and palm subdomains)., Unge T, Knight S, Bhikhabhai R, Lovgren S, Dauter Z, Wilson K, Strandberg B, Structure. 1994 Oct 15;2(10):953-61. PMID:7532533
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