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 language | English |
|---|---|
| Pages (from-to) | 310-315 |
| Number of pages | 6 |
| Journal | Nature |
| Volume | 302 |
| Issue number | 5906 |
| DOIs | |
| State | Published - May 5 1983 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Gene and protein structure of a β-crystallin polypeptide in murine lens
T2 - Relationship of exons and structural motifs
AU - Inana, George
AU - Piatigorsky, J.
AU - Norman, B.
AU - Slingsby, C.
AU - Blundell, T.
PY - 1983/5/5
Y1 - 1983/5/5
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0020695877&partnerID=8YFLogxK
U2 - 10.1038/302310a0
DO - 10.1038/302310a0
M3 - Article
C2 - 6835368
AN - SCOPUS:0020695877
VL - 302
SP - 310
EP - 315
JO - Nature
JF - Nature
SN - 0028-0836
IS - 5906
ER -