Gene and protein structure of a β-crystallin polypeptide in murine lens: Relationship of exons and structural motifs

George Inana, J. Piatigorsky, B. Norman, C. Slingsby, T. Blundell

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

A 23,000 molecular weight β-crystallin (β23) of the murine 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 γ(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 β- and γ-crystallin polypeptides, and link gene structure with protein structure in this superfamily of lens proteins.

Original languageEnglish
Pages (from-to)310-315
Number of pages6
JournalNature
Volume302
Issue number5906
DOIs
StatePublished - May 5 1983
Externally publishedYes

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Crystallins
Lenses
Exons
Peptides
Proteins
Computer Graphics
Tertiary Protein Structure
Introns
Genes
Molecular Weight
Membranes

ASJC Scopus subject areas

  • General

Cite this

Gene and protein structure of a β-crystallin polypeptide in murine lens : Relationship of exons and structural motifs. / Inana, George; Piatigorsky, J.; Norman, B.; Slingsby, C.; Blundell, T.

In: Nature, Vol. 302, No. 5906, 05.05.1983, p. 310-315.

Research output: Contribution to journalArticle

Inana, George ; Piatigorsky, J. ; Norman, B. ; Slingsby, C. ; Blundell, T. / Gene and protein structure of a β-crystallin polypeptide in murine lens : Relationship of exons and structural motifs. In: Nature. 1983 ; Vol. 302, No. 5906. pp. 310-315.
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