The LIM domain is a modular protein-binding interface.
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.
Biology Department, University of Utah, Salt Lake City 84112.
K L
KL
Schmeichel
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MC
Beckerle
D000185:Actinin / Q000378:metabolism; D000595:Amino Acid Sequence; D030161:Avian Proteins; D002448:Cell Adhesion; D003001:Cloning, Molecular; D016384:Consensus Sequence; D003545:Cysteine / Q000737:chemistry; D066298:In Vitro Techniques; D008667:Metalloproteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000378:metabolism*; D011485:Protein Binding; D016271:Proto-Oncogene Proteins c-myc / Q000378:metabolism*; D011993:Recombinant Fusion Proteins; D017384:Sequence Deletion; D013329:Structure-Activity Relationship
D030161:Avian Proteins; D008667:Metalloproteins; D009124:Muscle Proteins; D016271:Proto-Oncogene Proteins c-myc; D011993:Recombinant Fusion Proteins; C081447:cysteine-rich protein, avian; D000185:Actinin; D003545:Cysteine