The LIM/double zinc-finger motif functions as a protein dimerization domain.

Protein-protein interactions resulting in dimerization and heterodimerization are of central importance in the control of gene expression and cell function. Proteins that share the 52-residue LIM/double zinc-finger domain are involved in a wide range of developmental and cellular controls. Some of these functions have been hypothesized to involve protein dimerization. ...
In the present report we demonstrate, using both in vitro and cell-based studies, that a representative LIM protein, human cysteine-rich protein (hCRP), can efficiently homodimerize. The dimerization ability of hCRP is mapped to the LIM domains, can be transferred to an unrelated protein by fusion of a single minimal LIM/double zinc-finger segment, occurs in the absence as well as the presence of DNA, and appears to depend on coordination of two zinc atoms in the finger doublet. These observations support a specific role for protein dimerization in the function of proteins containing the LIM/double zinc-finger domain and expand the general spectrum of potential interactions mediated by zinc-finger motifs.
Mesh Terms:
Amino Acid Sequence, Antibodies, Cloning, Molecular, DNA-Binding Proteins, Glutathione Transferase, Humans, Macromolecular Substances, Molecular Sequence Data, Mutagenesis, Site-Directed, Nuclear Proteins, Protein Conformation, Protein Multimerization, Proteins, Proto-Oncogene Proteins c-myc, Recombinant Fusion Proteins, TATA Box, Transcriptional Activation, Zinc Fingers
Proc. Natl. Acad. Sci. U.S.A.
Date: Oct. 25, 1994
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