ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
The crystal structure of prolyl-glutaminyl-valyl-statyl-alanyl-leucine (Pro-Gln-Val-Sta-Ala-Leu, C32H57N709.5H20, Mr = 683.9 + 90.1), a putative HTLV-1 protease inhibitor based on one of the consensus retroviral protease cleavage sequences, and containing the statine residue [(4S,3S)-4-amino-3-hydroxy-6-methylheptanoic acid], has been determined by X-ray diffraction. The same molecule has been modelled in the active site of the HTLV-1 protease and both conformations have been compared. The peptide crystallizes as a pentahydrate in space group P21 with a = 10.874(2), b = 9.501(2), c = 21.062(5) Å, β = 103.68 (1)°, Z = 2, V= 2114.3 Å3, Dx = 1.21 g cm−3, μ = 8.02 cm−1, T= 293 K, λ(Cu Kα) = 1.5418 Å. The structure has been refined to an R value of 0.070 for 2152 observed reflections. The peptide main chain can be described as extended and adopts the usual zigzag conformation from the prolyl to the statyl residue. The main difference in conformation between the individual observed and modelled molecules is located on the Sta, Ala and Leu residues with the main chain of the modelled molecule rotated by about 180° as compared to the observed conformation in the crystal state.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444992013623
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