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Structure of Bovine Eye Lens γD (γIIIb)-Crystallin at 1.95 Å (1996)

Chirgadze, Y. N. ; Driessen, H. P. C. ; Wright, G. ; [et al.]

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 52 (1996), S. 712-721

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ISSN: 1399-0047

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: The crystal structure of bovine lens γIIIb-crystallin at 2.5 Å resolution previously reported was interpreted using a consensus sequence derived from related vertebrate sequences on the assumption that γIIIb-crystallin derived from the γC-crystallin gene. It has recently been shown that γIIIb is a product of the bovine γD gene. The structure of γIIIb has now been refined with the bovine γD sequence using new 1.95 Å resolution synchrotron data. The crystallographic R factor was 20.4% for all 33 104 reflection data between 8.0 and 1.95 Å measured at 277(1) K. The electron density fully supported the assignment of the γD sequence to γIIIb. The crystal belongs to space group P212121 with two molecules of molecular mass 20 749 Da in the asymmetric unit in which 219 water molecules were located. The two-domain four-Greek-key motif highly symmetrical protein is very similar in structure to γB-crystallin (81% sequence identity). There is a single amino-acid deletion in γD in the linker region connecting the two domains. The intermolecular oganization in the crystal lattice is quite different from γB as a result of key mutations involving surface residues Leu51, Ile103 and His155. These point mutations will contribute to the intermolecular behaviour of the γ-crystallins in the eye lens, where they are major components of the densely packed, high refractive index regions of the lens.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1107/S0907444996000352

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Surface interactions of γ-crystallins in the crystal medium in relation to their association in the eye lens (1988)

Sergeev, Y. V. ; Chirgadze, Y. N. ; Mylvaganam, S. E. ; [et al.]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 4 (1988), S. 137-147

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ISSN: 0887-3585

Keywords: eye lens proteins ; protein association ; crystal packing ; surface area ; homologous proteins ; point mutations ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: A comparative study of intermolecular interactions in crystals of two homologous low molecular weight proteins, γ-II and γ-IIIb crystallins, from calf eye lens was carried out. Crystal packings for these proteins are very different: intermolecular contact areas compose about 33% of the total accessible surface area of γ-II as compared with 13% in γ-III. Two key residues seem to be mainly responsible for the differences in protein association in the crystal medium. These are Ser 103 and Leu 155 in γ-II, which are replaced by Met 103 and His 155 in γ-IIIb. A similar substitution of these residues is observed in different gene products of γ-crystallins from a number of vertebrates. This is consistent with the existence of a genetically controlled mechanism for determining intermolecular association of γ-crystallins in the native medium of the lens.

Additional Material: 4 Ill.