2R8N

Structural Analysis of the Unbound Form of HIV-1 Subtype C Protease

Summary for 2R8N

• Entry DOI: 10.2210/pdb2r8n/pdb
• Descriptor: Pol protein, GLYCEROL (3 entities in total)
• Functional Keywords: hiv-1 subtype c, aspartyl protease, hydrolase, multifunctional enzyme, nucleotidyltransferase, protease, rna-directed dna polymerase, transferase
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 1
• Total formula weight: 10935.98

Authors

Coman, R.M.,Robbins, A.H.,McKenna, R.,Dunn, B.M. (deposition date: 2007-09-11, release date: 2008-07-29, Last modification date: 2024-02-21)

Primary citation

Coman, R.M.,Robbins, A.H.,Goodenow, M.M.,Dunn, B.M.,McKenna, R.
High-resolution structure of unbound human immunodeficiency virus 1 subtype C protease: implications of flap dynamics and drug resistance.
Acta Crystallogr.,Sect.D, 64:754-763, 2008

PubMed Abstract: The X-ray crystal structure of the unbound state of human immunodeficiency virus 1 (HIV-1) subtype C protease (C PR) has been determined to 1.20 angstroms resolution in the tetragonal space group P4(1)2(1)2, with one monomer per asymmetric unit and unit-cell parameters a = 46.7, c = 100.8 angstroms, allowing full anisotropic least-squares refinement. The refined model has a conventional R factor of 14.1% for all reflections and estimated standard deviations in bond lengths and angles for all main-chain non-H atoms of 0.014 angstroms and 0.030 degrees , respectively. The structure is compared with three unbound subtype B proteases (B PRs) to identify structural changes arising from the naturally occurring polymorphisms and delineate their implications in antiretroviral drug resistance/susceptibility. The unbound C PR exhibits a larger distance between the tips of the flaps, a downward displacement of the 36-41 loop and an increased thermal stability of the 10s loop when compared with the B PR structures. The C PR structure presents the highest resolution of the unbound state of a non-subtype-B PR and adds to the understanding of flap dynamics and drug resistance.

PubMed: 18566511
DOI: 10.1107/S090744490801278X

Experimental method

X-RAY DIFFRACTION (1.2 Å)