Abstract：
:LIM domains are zinc-binding protein sequences that are found in a growing number of proteins, including certain transcriptional regulators, proto-oncogene products, and adhesion plaque constituents. Here we define the biological activity of the LIM domain through studies of an adhesion plaque protein called zyxin that displays three C-terminal LIM domains. We have used our ability to reconstitute complexes between zyxin and its two known binding partners, alpha-actinin and the cysteine-rich protein (CRP), to examine the involvement of LIM domains in protein-protein interactions. We have determined that one of the three LIM domains of zyxin is necessary and sufficient to support the association of zyxin with CRP. Our findings demonstrate that the LIM domain functions as a specific protein-binding interface.
journal_name
Celljournal_title
Cellauthors
Schmeichel KL,Beckerle MCdoi
10.1016/0092-8674(94)90191-0subject
Has Abstractpub_date
1994-10-21 00:00:00pages
211-9issue
2eissn
0092-8674issn
1097-4172pii
0092-8674(94)90191-0journal_volume
79pub_type
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