Domain interactions and connecting peptides in lens crystallins
| Autor: | Eva-Maria Mayr, Rainer Jaenicke, Rudi Glockshuber |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular Macromolecular Substances Protein Conformation Stereochemistry Molecular Sequence Data Context (language use) Peptide Turn (biochemistry) Protein structure Drug Stability Structural Biology Crystallin Lens Crystalline Animals Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification Binding Sites Chemistry Crystallins eye diseases Cattle Protein folding sense organs Linker Protein Binding |
| Zdroj: | Journal of Molecular Biology. 235:84-88 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/s0022-2836(05)80017-8 |
| Popis: | beta B2- and gamma B-crystallin from bovine eye-lens are closely related proteins, topologically distinct mainly by virtue of the linker peptide connecting the two domains in each polypeptide chain. In homodimeric beta B2-crystallin, the extended conformation of the connecting peptide has been suggested to force the beta B2-molecule to favor intermolecular domain interactions compared with intramolecular contacts in monomeric gamma B-crystallin. From this one may postulate that the conserved interdomain contacts are essential for the overall stability of crystallins. This was clearly confirmed for gamma B-crystallin, since its isolated C-terminal domain is significantly less stable than in the context of native gamma B. Exchanging the linker peptide of gamma B- for that of beta B2-crystallin yields a monomeric protein with stability characteristics identical to gamma B-crystallin. We conclude that the domain-interface itself rather than the connecting peptide determines the mode of domain association in crystallins, as the linker in the gamma B beta-mutant is evidently twisted to a turn similar to the one in natural gamma B-crystallin. |
| Databáze: | OpenAIRE |
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