Structure of the unbound form of HIV-1 subtype A protease: comparison with unbound forms of proteases from other HIV subtypes.
Acta Crystallogr D Biol Crystallogr
; 66(Pt 3): 233-42, 2010 Mar.
Article
en En
| MEDLINE
| ID: mdl-20179334
ABSTRACT
The crystal structure of the unbound form of HIV-1 subtype A protease (PR) has been determined to 1.7 A resolution and refined as a homodimer in the hexagonal space group P6(1) to an R(cryst) of 20.5%. The structure is similar in overall shape and fold to the previously determined subtype B, C and F PRs. The major differences lie in the conformation of the flap region. The flaps in the crystal structures of the unbound subtype B and C PRs, which were crystallized in tetragonal space groups, are either semi-open or wide open. In the present structure of subtype A PR the flaps are found in the closed position, a conformation that would be more anticipated in the structure of HIV protease complexed with an inhibitor. The amino-acid differences between the subtypes and their respective crystal space groups are discussed in terms of the differences in the flap conformations.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Proteasa del VIH
/
VIH-1
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Año:
2010
Tipo del documento:
Article
País de afiliación:
Estados Unidos