1rtd

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[[Image:1rtd.gif|left|200px]]<br /><applet load="1rtd" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rtd.gif|left|200px]]
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caption="1rtd, resolution 3.2&Aring;" />
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'''STRUCTURE OF A CATALYTIC COMPLEX OF HIV-1 REVERSE TRANSCRIPTASE: IMPLICATIONS FOR NUCLEOSIDE ANALOG DRUG RESISTANCE'''<br />
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{{Structure
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|PDB= 1rtd |SIZE=350|CAPTION= <scene name='initialview01'>1rtd</scene>, resolution 3.2&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=TTP:THYMIDINE-5'-TRIPHOSPHATE'>TTP</scene>
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|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]
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|GENE= POL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1])
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}}
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'''STRUCTURE OF A CATALYTIC COMPLEX OF HIV-1 REVERSE TRANSCRIPTASE: IMPLICATIONS FOR NUCLEOSIDE ANALOG DRUG RESISTANCE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1RTD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=TTP:'>TTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RTD OCA].
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1RTD is a [[Protein complex]] structure of sequences 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=1RTD OCA].
==Reference==
==Reference==
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Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance., Huang H, Chopra R, Verdine GL, Harrison SC, Science. 1998 Nov 27;282(5394):1669-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9831551 9831551]
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Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance., Huang H, Chopra R, Verdine GL, Harrison SC, Science. 1998 Nov 27;282(5394):1669-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9831551 9831551]
[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: protein/dna]]
[[Category: protein/dna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:54:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:55:55 2008''

Revision as of 11:56, 20 March 2008


PDB ID 1rtd

Drag the structure with the mouse to rotate
, resolution 3.2Å
Ligands: and
Gene: POL (Human immunodeficiency virus 1)
Activity: RNA-directed DNA polymerase, with EC number 2.7.7.49
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF A CATALYTIC COMPLEX OF HIV-1 REVERSE TRANSCRIPTASE: IMPLICATIONS FOR NUCLEOSIDE ANALOG DRUG RESISTANCE


Overview

A combinatorial disulfide cross-linking strategy was used to prepare a stalled complex of human immunodeficiency virus-type 1 (HIV-1) reverse transcriptase with a DNA template:primer and a deoxynucleoside triphosphate (dNTP), and the crystal structure of the complex was determined at a resolution of 3.2 angstroms. The presence of a dideoxynucleotide at the 3'-primer terminus allows capture of a state in which the substrates are poised for attack on the dNTP. Conformational changes that accompany formation of the catalytic complex produce distinct clusters of the residues that are altered in viruses resistant to nucleoside analog drugs. The positioning of these residues in the neighborhood of the dNTP helps to resolve some long-standing puzzles about the molecular basis of resistance. The resistance mutations are likely to influence binding or reactivity of the inhibitors, relative to normal dNTPs, and the clustering of the mutations correlates with the chemical structure of the drug.

About this Structure

1RTD is a Protein complex structure of sequences from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance., Huang H, Chopra R, Verdine GL, Harrison SC, Science. 1998 Nov 27;282(5394):1669-75. PMID:9831551

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