View source for 4id5

==HIV-1 reverse transcriptase with bound fragment at the RNase H primer grip site==
<StructureSection load='4id5' size='340' side='right' caption='[[4id5]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4id5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_bh10 Human immunodeficiency virus type 1 bh10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ID5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ID5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1FF:1-METHYL-5-PHENYL-1H-PYRAZOLE-4-CARBOXYLIC+ACID'>1FF</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=T27:4-{[4-({4-[(E)-2-CYANOETHENYL]-2,6-DIMETHYLPHENYL}AMINO)PYRIMIDIN-2-YL]AMINO}BENZONITRILE'>T27</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4icl|4icl]], [[4idk|4idk]], [[4ify|4ify]], [[4ig0|4ig0]], [[4ig3|4ig3]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag-pol, POL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11678 Human immunodeficiency virus type 1 BH10])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4id5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4id5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4id5 RCSB], [http://www.ebi.ac.uk/pdbsum/4id5 PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
HIV-1 reverse transcriptase (RT) plays an essential role in viral replication and is an attractive target for antiretroviral therapy. RT, a p66/p51 heterodimer, is a multi-domain protein that undergoes a series of conformational changes during the replication of the HIV-1 genome. The intrinsic flexibility of RT can provide novel allosteric sites for inhibition. Crystals of RT that diffract X-rays to better than 2 A resolution facilitated the probing of RT for new druggable sites using X-ray crystallographic fragment screening. A total of 775 fragments were grouped into 143 cocktails, which were soaked into crystals of RT in complex with the non-nucleoside drug Edurant (TMC278/rilpivirine). Fragment binding was observed at seven new binding sites. These include the incoming nucleotide binding, Knuckles, NNRTI Adjacent, and 399 sites, located in the polymerase region of RT, and the 428, RNase H primer grip adjacent, and 507 sites, located in the RNase H region. Three of these sites-Knuckles, NNRTI adjacent, and the incoming nucleotide binding-are inhibitory and provide opportunities for discovery of new anti-AIDS drugs.

Detecting allosteric sites of HIV-1 reverse transcriptase by X-ray crystallographic fragment screening.,Bauman JD, Patel D, Dharia C, Fromer M, Ahmed S, Frenkel Y, Eck JT, Ho W, Das K, Shatkin A, Arnold E J Med Chem. 2013 Jan 23. PMID:23342998<ref>PMID:23342998</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>

==See Also==
*[[Reverse transcriptase|Reverse transcriptase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human immunodeficiency virus type 1 bh10]]
[[Category: Arnold, E]]
[[Category: Bauman, J D]]
[[Category: Patel, D]]
[[Category: Dna polymerase]]
[[Category: Endonuclease]]
[[Category: Hydrolase]]
[[Category: Multifunctional enzyme]]
[[Category: Rna-directed dna polymerase]]
[[Category: Transferase-transferase inhibitor complex]]