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. 1985 Oct;4(10):2597–2602. doi: 10.1002/j.1460-2075.1985.tb03976.x

beta s-Crystallin: structure and evolution of a distinct member of the beta gamma-superfamily.

Y Quax-Jeuken, H Driessen, J Leunissen, W Quax, W de Jong, H Bloemendal
PMCID: PMC554549  PMID: 4054100

Abstract

The nucleotide sequence of the cDNA of bovine lens beta s-crystallin has been determined, and the derived amino acid sequence has been confirmed by amino acid compositions and partial sequences of the tryptic peptides of this monomeric protein. beta s-Crystallin has a length of 177 residues, corresponding to a mol. wt. of 20 773, and a blocked N-terminal serine. Comparison of beta s with the known sequences of other beta- and gamma-crystallins, and computer construction of a phylogenetic tree of these sequences, shows beta s to be more closely related to the monomeric gamma-crystallins than to the oligomeric beta-crystallins. Also the tertiary structure of beta s modelled by interactive computer graphics on the coordinates of gamma II-crystallin, revealed similarities with the gamma-crystallins which might explain its monomeric behavior: the presence of a very short N-terminal 'arm' as compared with the beta-crystallins; a distribution of charged residues on the surface as in the gamma-crystallins; and finally the nature of certain residues of its inter-domain contacts. beta s-Crystallin seems to be an old and isolated offshoot of the gamma-family, and, considering its ancient origin, might well be present in other, non-mammalian, vertebrate classes.

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Selected References

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