期刊
CELL MOTILITY AND THE CYTOSKELETON
卷 52, 期 1, 页码 9-21出版社
WILEY-LISS
DOI: 10.1002/cm.10027
关键词
villin headpiece; dematin; villidin; supervillin; actin-binding; surface potential
类别
资金
- NHLBI NIH HHS [HL-51445, HL07291] Funding Source: Medline
- NIGMS NIH HHS [GM33048, GM62886, R01 GM033048] Funding Source: Medline
The villin-type headpiece domain is a modular motif found at the extreme C-terminus of larger core domains in over 25 cytoskeletal proteins in plants and animals. Although headpiece is classified as an F-actin-binding domain, it has been suggested that some expressed fusion-proteins containing headpiece may lack F-actin-binding in vivo. To determine the intrinsic F-actin affinity of headpiece domains, we quantified the F-actin affinity of seven headpiece domains and three N-terminal truncations, under identical in vitro conditions. The constructs are folded and adopt the native headpiece structure. However, they show a wide range of affinities that can be grouped into high, low, and nonspecific-binding categories. Computer models of the structure and charged surface potential of these headpiece domains suggest features important for high F-actin affinity. We conclude that not all headpiece domains are intrinsically F-actin-binding motifs, and suggest that the surface charge distribution may be an important element for F-actin recognition. (C) 2002 Wiley-Liss, Inc.
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