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InterPro: IPR001064 Beta/gamma crystallin

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684 proteins

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Accession

IPR001064 Beta/gamma_crystallin

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:2.60.20.10	Crystallin	628
Pfam	PF00030	Crystall	444
PRINTS	PR01367	BGCRYSTALLIN	381
PROSITE profile	PS50915	CRYSTALLIN_BETA_GAMMA	610
SMART	SM00247	XTALbg	530
Signatures in BioMart

InterPro Relationships Help

Parent

IPR011024 Gamma-crystallin related

InterPro annotation

Entry Details in BioMart

Abstract

The crystallins are water-soluble structural proteins that occur in high concentration in the cytoplasm of eye lens fiber cells. Four major groups of crystallin 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].

This entry represents beta and gamma- crystallin which form a family of related proteins [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.

Structural links Help

PDB - click here

SCOP: b.11.1.1

CATH: 2.60.20.10

Database links Help

PROSITE doc: PDOC00197

PANDIT: PF00030

Blocks: IPB001064

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001064

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35486 Beta-crystallin S

P02522 Beta-crystallin B2

P02966 Development-specific protein S

P07316 Gamma-crystallin B

P09353 Spherulin-3A

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011024	Gamma-crystallin related
IPR001064	Beta/gamma crystallin
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	de Jong WW, Hendriks W, Mulders JW, Bloemendal H. Evolution of eye lens crystallins: the stress connection. Trends Biochem. Sci. 14 365-8 1989 [PubMed: 2688200] http://dx.doi.org/10.1016/0968-0004(89)90009-1
2.	Simpson A, Bateman O, Driessen H, Lindley P, Moss D, Mylvaganam S, Narebor E, Slingsby C. The structure of avian eye lens delta-crystallin reveals a new fold for a superfamily of oligomeric enzymes. Nat. Struct. Biol. 1 724-34 1994 [PubMed: 7634077] http://dx.doi.org/10.1038/nsb1094-724
3.	Wistow G. Evolution of a protein superfamily: relationships between vertebrate lens crystallins and microorganism dormancy proteins. J. Mol. Evol. 30 140-5 1990 [PubMed: 2107329] http://dx.doi.org/10.1007/BF02099940
4.	Lubsen NH, Aarts HJ, Schoenmakers JG. The evolution of lenticular proteins: the beta- and gamma-crystallin super gene family. Prog. Biophys. Mol. Biol. 51 47-76 1988 [PubMed: 3064189] http://dx.doi.org/10.1016/0079-6107(88)90010-7

Additional Reading Open in usermanual
	Palme S, Jaenicke R, Slingsby C. X-ray structures of three interface mutants of gammaB-crystallin from bovine eye lens. Protein Sci. 7 1998 611-8 [PubMed: 9541393] http://www.proteinscience.org/cgi/content/abstract/7/3/611
	Slingsby C, Bateman OA. Quaternary interactions in eye lens beta-crystallins: basic and acidic subunits of beta-crystallins favor heterologous association. Biochemistry 29 1990 6592-9 [PubMed: 2397202] http://dx.doi.org/10.1021/bi00480a007
	Kroone RC, Elliott GS, Ferszt A, Slingsby C, Lubsen NH, Schoenmakers JG. The role of the sequence extensions in beta-crystallin assembly. Protein Eng. 7 1994 1395-9 [PubMed: 7700872] http://dx.doi.org/10.1093/protein/7.11.1395
	Smith MA, Bateman OA, Jaenicke R, Slingsby C. Mutation of interfaces in domain-swapped human betaB2-crystallin. Protein Sci. 16 2007 615-25 [PubMed: 17327390] http://dx.doi.org/10.1110/ps.062659107
	Carver JA. Probing the structure and interactions of crystallin proteins by NMR spectroscopy. 18 1999 431-62 [PubMed: 10217479] http://dx.doi.org/10.1016/S1350-9462(98)00027-5
	Purkiss AG, Bateman OA, Wyatt K, Wilmarth PA, David LL, Wistow GJ, Slingsby C. Biophysical properties of gammaC-crystallin in human and mouse eye lens: the role of molecular dipoles. J. Mol. Biol. 372 2007 205-22 [PubMed: 17659303] http://dx.doi.org/10.1016/j.jmb.2007.06.049
	Ray ME, Wistow G, Su YA, Meltzer PS, Trent JM. AIM1, a novel non-lens member of the betagamma-crystallin superfamily, is associated with the control of tumorigenicity in human malignant melanoma. Proc. Natl. Acad. Sci. U.S.A. 94 1997 3229-34 [PubMed: 9096375] http://dx.doi.org/10.1073/pnas.94.7.3229
	Ebersbach H, Fiedler E, Scheuermann T, Fiedler M, Stubbs MT, Reimann C, Proetzel G, Rudolph R, Fiedler U. Affilin-novel binding molecules based on human gamma-B-crystallin, an all beta-sheet protein. J. Mol. Biol. 372 2007 172-85 [PubMed: 17628592] http://dx.doi.org/10.1016/j.jmb.2007.06.045
	Grishaev A, Wu J, Trewhella J, Bax A. Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data. J. Am. Chem. Soc. 127 2005 16621-8 [PubMed: 16305251] http://dx.doi.org/10.1021/ja054342m
	Wistow GJ, Piatigorsky J. Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Annu. Rev. Biochem. 57 1988 479-504 [PubMed: 3052280] http://dx.doi.org/10.1146/annurev.bi.57.070188.002403
	Artero JB, Hartlein M, McSweeney S, Timmins P. A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O. Acta Crystallogr. D Biol. Crystallogr. 61 2005 1541-9 [PubMed: 16239733] http://dx.doi.org/10.1107/S0907444905028532
	Rath VL, Fletterick RJ. Parallel evolution in two homologues of phosphorylase. Nat. Struct. Biol. 1 1994 681-90 [PubMed: 7634071] http://dx.doi.org/10.1038/nsb1094-681
	Real and artificial histories. Nat. Struct. Biol. 1 1994 655-6 [PubMed: 7543359]

InterPro 23.1