Abstract:
:The crystal structure of human immunodeficiency virus type 1 (HIV-1) protease mutant G48H with peptidic inhibitor U-89360E is described. Comparison with wild-type protease-inhibitor complex shows that mutation of flap residue 48 to histidine allows stabilizing van der Waals contacts between the side chains of His48 and Phe53 as well as between His48 and the P2' and P3' inhibitor subsites. The flap region is less mobile than in the wild-type enzyme. A model of saquinavir-resistant mutant protease G48V in complex with saquinavir predicts interactions similar to those found in the G48H crystal. Energetic calculations confirm the similarity of the His48 and Val48 interactions.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hong L,Zhang XJ,Foundling S,Hartsuck JA,Tang Jdoi
10.1016/s0014-5793(97)01477-4subject
Has Abstractpub_date
1997-12-22 00:00:00pages
11-6issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(97)01477-4journal_volume
420pub_type
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