RELAXATION STUDY OF THE BACKBONE DYNAMICS OF HUMAN PROFILIN BY 2-DIMENSIONAL H-1-N-15 NMR

被引:7
作者
CONSTANTINE, KL [1 ]
FRIEDRICHS, MS [1 ]
BELL, AJ [1 ]
LAVOIE, TB [1 ]
MUELLER, L [1 ]
METZLER, WJ [1 ]
机构
[1] BRISTOL MYERS SQUIBB PHARMACEUT RES INST,DEPT MACROMOLEC BIOCHEM,PRINCETON,NJ 08543
关键词
ACTIN-BINDING PROTEIN; CONFORMATIONAL CHANGE; NMR RELAXATION; ORDER PARAMETER; POLY-L-PROLINE BINDING;
D O I
10.1016/0014-5793(93)80855-O
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The dynamic properties of 111 backbone HN sites in uncomplexed human profilin, a protein of 139 residues, have been characterized by two-dimensional inverse-detected H-1-N-15 NMR spectroscopy. Heteronuclear {H-1}-N-15 nuclear Overhauser effects and N-15 longitudinal and transverse relaxation rates have been analyzed in terms of model-free spectral density functions and exchange contributions to transverse relaxation rates. Relatively high mobilities on the nanosecond timescale are observed for Asp(26) and Ser(27), which form part of a loop connecting beta-strands A and B, and for Thr(92) through Ala(95), which are in a loop connecting beta-strands E and F. Significant exchange contributions, indicative of motions on the microsecond to millisecond timescale, have been obtained for 30 residues. These include Leu(77), Asp(80) and Gly(81) of a loop between beta-strands D and E, Ser(84) and Met(85) of beta-strand E, Gly(121) of a loop connecting beta-strand G and the C-terminal helix, and Gln(138), which is next to the C-terminal residue Tyr(139). Some of the regions showing high flexibility in profilin are known to be involved in poly-L-proline binding.
引用
收藏
页码:457 / 461
页数:5
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