Norledge, B. V. and Mayr, E.-M. and Glockshuber, R. and Bateman, O. A. and Slingsby, C. and Jaenicke, Rainer and Driessen, H. P. C. (1996) The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins. NATURE STRUCTURAL BIOLOGY, 3 (3). pp. 267-274. ISSN 1072-8368
Full text not available from this repository.Abstract
We use protein engineering and crystallography to simulate aspects of the early evolution of beta gamma-crystallins by observing how a single domain oligomerizes in response to changes in a sequence extension. The crystal structure of the C-terminal domain of gamma B-crystallin with its four-residue C-terminal extension shows that the domain does not form a symmetric homodimer analogous to the two-domain pairing in beta gamma-crystallins. Instead the C-terminal extension now forms heterologous interactions with other domains leading to the solvent exposure of the natural hydrophobic interface with a consequent loss in protein solubility. However, this domain truncated by just the C-terminal tyrosine forms a symmetric homodimer of domains in the crystal lattice.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | EYE LENS; BETA-B2-CRYSTALLIN; CELL; UNIT |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 07 Nov 2023 10:02 |
| Last Modified: | 07 Nov 2023 10:02 |
| URI: | https://pred.uni-regensburg.de/id/eprint/51900 |
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