In:
Acta Crystallographica Section D Biological Crystallography, International Union of Crystallography (IUCr), Vol. 66, No. 3 ( 2010-03-01), p. 233-242
Abstract:
The crystal structure of the unbound form of HIV-1 subtype A protease (PR) has been determined to 1.7 Å resolution and refined as a homodimer in the hexagonal space group P 6 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.
Type of Medium:
Online Resource
ISSN:
0907-4449
DOI:
10.1107/S0907444909054298
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2010
detail.hit.zdb_id:
2968623-4
SSG:
12
SSG:
13
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