Beta gamma crystallin

Beta gamma crystallin
Beta/Gamma crystallin
Identifiers
Symbol Crystall
Pfam PF00030
InterPro IPR001064
PROSITE PDOC00197
SCOP 4gcr

βγ-Crystallin is a family of β- and γ-crystallin proteins from vertebrate eye lens.

The crystallins are water-soluble structural proteins that occur in high concentration in the cytoplasm of eye lens fiber cells. Four major groups of crystallins have been distinguished on the basis of size, charge and immunological properties: alpha-, beta- and gamma-crystallins occur in all vertebrate classes (though gamma-crystallins are low or absent in avian lenses); and delta-crystallin is found exclusively in reptiles and birds[1][2].

Beta and gamma- crystallin form a separate family [3][4]. Structurally, beta and gamma crystallins are composed of two similar domains which, in turn, are each composed of two similar motifs with the two domains connected by a short connecting peptide. Each motif, which is about forty amino acid residues long, is folded in a distinctive Greek key pattern. However, beta crystallin is an oligomer, composed of a complex group of molecules, whereas gamma cryallin is a simpler monomer.[5]

Human proteins containing this domain

AIM1; AIM1L; CRYBA1; CRYBA2; CRYBA4; CRYBB1; CRYBB2; CRYBB3; CRYGA; CRYGB; CRYGC; CRYGD; CRYGN; CRYGS;

References

  1. ^ de Jong WW, Bloemendal H, Hendriks W, Mulders JW (1989). "Evolution of eye lens crystallins: the stress connection". Trends Biochem. Sci. 14 (9): 365–368. doi:10.1016/0968-0004(89)90009-1. PMID 2688200. 
  2. ^ Simpson A, Bateman O, Driessen H, Lindley P, Moss D, Mylvaganam S, Narebor E, Slingsby C (1994). "The structure of avian eye lens delta-crystallin reveals a new fold for a superfamily of oligomeric enzymes". Nat. Struct. Biol. 1 (10): 724–734. doi:10.1038/nsb1094-724. PMID 7634077. 
  3. ^ Wistow G (1990). "Evolution of a protein superfamily: relationships between vertebrate lens crystallins and microorganism dormancy proteins". J. Mol. Evol. 30 (2): 140–145. doi:10.1007/BF02099940. PMID 2107329. 
  4. ^ Schoenmakers JG, Lubsen NH, Aarts HJ (1988). "The evolution of lenticular proteins: the beta- and gamma-crystallin super gene family". Prog. Biophys. Mol. Biol. 51 (1): 47–76. doi:10.1016/0079-6107(88)90010-7. PMID 3064189. 
  5. ^ Nathaniel Knox Cartwright, Petros Carvounis (2005). Short answer questions for the MRCOphth, Part 1. Radcliffe Publishing. p. 80. http://books.google.com/books?id=5KslZLOs58gC&pg=PA80. 
v · Eye proteins
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Crystallin
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M: EYE

anat(g/a/p)/phys/devp/prot

noco/cong/tumr, epon

proc, drug(S1A/1E/1F/1L)

This article includes text from the public domain Pfam and InterPro IPR001064


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