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Publication : Gene and protein structure of a beta-crystallin polypeptide in murine lens: relationship of exons and structural motifs.

First Author  Inana G Year  1983
Journal  Nature Volume  302
Issue  5906 Pages  310-5
PubMed ID  6835368 Mgi Jnum  J:7022
Mgi Id  MGI:55493 Doi  10.1038/302310a0
Citation  Inana G, et al. (1983) Gene and protein structure of a beta-crystallin polypeptide in murine lens: relationship of exons and structural motifs. Nature 302(5906):310-5
abstractText  A 23,000 molecular weight beta-crystallin (beta 23) of the murine eye lens is encoded in a 4.1 +/- 0.3-kilobase gene containing three introns. Each of the four exons seems to code for a separate structural motif of the protein, whose tertiary structure was predicted by an interactive computer graphics technique based on the crystallographic structure of bovine gamma II-crystallin. The first exon also encodes a hydrophobic N-terminal peptide resembling membrane anchor sequences of other proteins. Our results indicate structural homology among the beta- and gamma-crystallin polypeptides, and link gene structure with protein structure in this superfamily of lens proteins.
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