The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins

Nature Structural Biology

Volumn 3, Issue 3, 1996, Pages 267-274

  Norledge, B V ^a   Mayr, E M ^b   Glockshuber, R ^b   Bateman, O A ^a   Slingsby, C ^a   Jaenicke, R ^b   Driessen, H P C ^a  

^a UNIVERSITY OF LONDON   (United Kingdom)

^b UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BETA CRYSTALLIN; GAMMA CRYSTALLIN; MUTANT PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; HYDROPHOBICITY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; SOLUBILITY; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

EID: 0029930180     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0396-267     Document Type: Article

References (16)

1. Dobson, C.M. Finding the right fold. Nature Struct. Biol. 2, 513-517 (1995).
2. Wistow, G.J. & Piatigorsky, J. Lens crystallins: The evolution and expression of proteins for a highly specialized tissue. Annu. Rev. Biochem. 57, 479-504 (1988).
3. Blundell, T. et al. The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II. Nature 289, 771-777 (1981).
4. Bloemendal, H. & de Jong, W.W. Lens proteins and their genes. Prog. Nucleic Acid Res. Mol. Biol. 41, 259-281 (1991).
5. Bax, B. et al. X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins. Nature 347, 775-780 (1990).
6. Lubsen, N.H., Aarts, H.J.M. & Schoenmakers, J.G.G. The evolution of lenticular proteins: the β- and γ-crystallin super gene family. Prog. Biophys. Molec. Biol. 51, 47-76 (1988).
7. Wistow, G. Evolution of a protein superfamily: relationships between vertebrate lens crystallins and microorganism dormancy proteins. J. Mol. Evol. 30, 140-145 (1990).
8. Bennett, M.J., Choe, S. & Eisenberg, D. Domain swapping: entangling alliances between proteins. Proc Natl. Acad. Sci. USA 91, 3127-3131 (1994).
9. Slingsby, C., Bateman, O.A. & Simpson, A. Motifs involved in protein-protein interactions. Mol. Biol. Rep. 17, 185-195 (1993).
10. Wang, J. et al. Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer. Proc. Natl. Acad. Sci. USA 91, 7242-7246 (1994).
11. Fletterick, R.J & Bazan, J.F. When one and one are not two. Nature Struct. Biol. 2, 721-723 (1995).
12. Bennett, M.J., Schlunegger, M.P. & Eisenberg, D. 3D Domain swapping - a mechanism for oligomer assembly. Protein Sci. 4, 2455-2468 (1995).
13. Mayr, E-M., Jaenicke, R. & Glockshuber, R. Domain interactions and connecting peptides in lens crystallins. J. Mol. Biol. 235, 84-88 (1994).
14. Rudolph, R., Siebendritt, R., Nesslauer, G., Sharma, A.K. & Jaenicke, R. Folding of an all-β protein: independent domain folding in γII-crystallin from calf lens. Proc. Natl. Acad. Sci. USA 87, 4625-3629 (1990).
15. Magalhaes, A., Maigret, B., Hoflack, J., Gomes, J.N.F. & Scheraga, H.A. Contribution of unusual arginine-arginine short-range interactions to stabilization and recognition in proteins. J. Protein Chem. 13, 195-215 (1994).
16. De Jong, W.W., Lubsen, N.H. & Kraft, H.J. Molecular evolution of the eye lens. Prog. Ret. Eye Res. 13, 391-442 (1994).