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Domain binding and function: The LIM domain was first identified in three developmentally regulated transcription factors Lin-1, Isl-1 and Mec-3. It consists of approximately 60 amino acids and has been identified in over 300 proteins from organisms ranging from yeast to humans. The LIM domain is a zincbinding, cysteine-rich motif consisting of two tandemly repeated zinc fingers. Unlike GATA-type zinc fingers, LIM domains do not seem to bind DNA but instead appear to mediate proteinÀprotein interactions. Functionally, LIM domainÀcontaining proteins have been implicated in a variety of biological processes including cell lineage specification, cytoskeletal organization and organ development. Some LIM domainÀcontaining proteins appear to function solely as adapters to bring together other components into a complex (i.e., LMO and CRP) while other LIM domain containing proteins clearly have other functions conferred by additional functional domains such as the DNA binding homeodomain or a catalytic kinase domain. In addition, certain LIM domains have been observed to form dimers with other LIM domains. An overall consensus LIM domain binding site has not been defined. Factors that confer the specificity of LIM domain interactions remain to be determined.
Structure Reference: Konrat, R. et al. (1997) J. Biol. Chem. 272(18), 12001À12007.
Examples of Domain Proteins:
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| C-terminal LIM domain from quail CRP2. | |
