1rti

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
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.
+
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.
==About this Structure==
==About this Structure==
Line 29: Line 29:
[[Category: hiv-1 reverse transcriptase]]
[[Category: hiv-1 reverse transcriptase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:49:59 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:54:20 2008''

Revision as of 12:54, 21 February 2008


1rti, resolution 3.0Å

Drag the structure with the mouse to rotate

HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR RT-INHIBITOR COMPLEXES

Overview

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.

About this Structure

1RTI is a Protein complex structure of sequences from Human immunodeficiency virus 1 with and as ligands. Active as RNA-directed DNA polymerase, with EC number 2.7.7.49 Full crystallographic information is available from OCA.

Reference

High resolution structures of HIV-1 RT from four RT-inhibitor complexes., Ren J, Esnouf R, Garman E, Somers D, Ross C, Kirby I, Keeling J, Darby G, Jones Y, Stuart D, et al., Nat Struct Biol. 1995 Apr;2(4):293-302. PMID:7540934

Page seeded by OCA on Thu Feb 21 14:54:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools