High resolution structures of HIV-1 RT from four RT-inhibitor complexes. Export

@article{citeulike:1382232, abstract = {We have determined the structures of four complexes of HIV-1 reverse transcriptase with non-nucleoside inhibitors, three fully refined at high resolution. The highest resolution structure is of the RT-nevirapine complex which has an R-factor of 0.186 and a root-mean-square bond length deviation of 0.015 A for all data to 2.2 A. The structures reveal a common mode of binding for these chemically diverse compounds. The common features of binding are largely hydrophobic interactions and arise from induced shape complementarity achieved by conformational rearrangement of the enzyme and conformational/configurational rearrangement of the compounds.}, address = {Laboratory of Molecular Biophysics, Oxford, UK.}, author = {Ren, J. and Esnouf, R. and Garman, E. and Somers, D. and Ross, C. and Kirby, I. and Keeling, J. and Darby, G. and Jones, Y. and Stuart, D.}, citeulike-article-id = {1382232}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/7540934}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=7540934}, comment = {the reference for 1rth}, issn = {1072-8368}, journal = {Nat Struct Biol}, keywords = {clanokinsa, hiv, protein, rt}, month = {April}, number = {4}, pages = {293--302}, posted-at = {2007-06-12 22:55:29}, priority = {1}, title = {High resolution structures of HIV-1 RT from four RT-inhibitor complexes.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/7540934}, volume = {2}, year = {1995} }

TY - JOUR ID - citeulike:1382232 L3 - citeulike-article-id:1382232 N2 - We have determined the structures of four complexes of HIV-1 reverse transcriptase with non-nucleoside inhibitors, three fully refined at high resolution. The highest resolution structure is of the RT-nevirapine complex which has an R-factor of 0.186 and a root-mean-square bond length deviation of 0.015 A for all data to 2.2 A. The structures reveal a common mode of binding for these chemically diverse compounds. The common features of binding are largely hydrophobic interactions and arise from induced shape complementarity achieved by conformational rearrangement of the enzyme and conformational/configurational rearrangement of the compounds. IS - 4 JF - Nat Struct Biol SN - 1072-8368 AD - Laboratory of Molecular Biophysics, Oxford, UK. EP - 302 TI - High resolution structures of HIV-1 RT from four RT-inhibitor complexes. VL - 2 SP - 293 KW - clanokinsa KW - hiv KW - protein KW - rt N1 - the reference for 1rth AU - Ren, J AU - Esnouf, R AU - Garman, E AU - Somers, D AU - Ross, C AU - Kirby, I AU - Keeling, J AU - Darby, G AU - Jones, Y AU - Stuart, D PY - 1995/04// UR - http://view.ncbi.nlm.nih.gov/pubmed/7540934 ER -