CHARACTERIZATION OF THE INTERACTION OF NATURAL PROLINE-RICH PEPTIDES WITH 5 DIFFERENT SH3 DOMAINS

被引:135
作者
VIGUERA, AR [1 ]
ARRONDO, JLR [1 ]
MUSACCHIO, A [1 ]
SARASTE, M [1 ]
SERRANO, L [1 ]
机构
[1] UNIV BASQUE COUNTRY, DEPT BIOQUIM & BIOL MOLEC, E-48080 BILBAO, SPAIN
关键词
D O I
10.1021/bi00202a011
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 interaction of six different proline-rich peptides with five SH3 domains has been investigated by using spectroscopic techniques. These peptides correspond to natural sequences and have been implicated in the interaction of some SH3 domains with other proteins. We have determined the K-d values for all of the possible combinations between the peptides and the SH3 domains. Low specificity and low affinity (> 5 mu M) are the most remarkable conclusions from these studies. None of the peptides tested here were found to bind with significant affinity to spectrin-SH3 or n-src-SH3. Abl-SH3 seems to be the most selective of the domains analyzed here, while Fyn-SH3 is the most promiscuous. CD and FTIR studies indicate that these peptides adopt to different extents a PPII-like structure in aqueous solution. However, analysis of the SH3 domain complexes with these peptides suggests that proline-rich peptides do not necessarily adopt an overall PPII structure over their entire length upon binding to the different SH3 domains.
引用
收藏
页码:10925 / 10933
页数:9
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