Structural and kinetic characterization of the simplified SH3 domain FP1

被引:17
|
作者
Yi, Q
Rajagopal, P
Klevit, RE
Baker, D
机构
[1] Univ Washington, Dept Biochem, Seattle, WA 98195 USA
[2] Univ Washington, Howard Hughes Med Inst, Seattle, WA 98195 USA
关键词
FP1; simplified SH3; folding kinetics; NMR structure;
D O I
10.1110/ps.0238603
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 simplified SH3 domain sequence, FP1, obtained in phage display selection experiments has an amino acid composition that is 95% Ile, Lys, Glu, Ala, Gly. Here we use NMR to investigate the tertiary structure of FP1. We find that the overall topology of FP1 resembles that of the src SH3 domain, the hydrogen-deuterium exchange and chemical shift perturbation profiles are similar to those of naturally occurring SH3 domains, and the N-15 relaxation rates are in the range of naturally occur-ring small proteins. Guided by the structure, we further simplify the FP1 sequence and compare the effects on folding kinetics of point mutations in FP1 and the wild-type src SH3 domain. The results suggest that the folding transition state of FP1 is similar to but somewhat less polarized than that of the wild-type src SH3 domain.
引用
收藏
页码:776 / 783
页数:8
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