Wright, G. and Basak, A. K. and Wieligmann, K. and Mayr, E. M. and Slingsby, C. (1998) Circular permutation of beta B2-crystallin changes the hierarchy of domain assembly. PROTEIN SCIENCE, 7 (6). pp. 1280-1285. ISSN 0961-8368,
Full text not available from this repository.Abstract
The py-crystallins form a superfamily of eye lens proteins comprised of multiple creek motifs that are symmetrically organized into domains and higher assemblies, in the beta B2-crystallin dimer each polypeptide folds into two similar domains that are related to monomeric gamma-crystallin by domain swapping. The crystal structure of the circularly permuted two-domain beta B2 polypeptide shows that permutation converts intermolecular domain pairing into intramolecular pairing. However, the dimeric permuted protein is, in fact, half a native tetramer. This result shows how the sequential order of domains in multi-domain proteins can affect quaternary domain assembly.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | X-RAY-ANALYSIS; EYE LENS; BETA-CRYSTALLIN; EVOLUTION; PROTEINS; PEPTIDE; MODEL; GENES; beta gamma-crystallin; circular permutation; domain swapping; domain swivelling; eye-lens protein; quaternary structure |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 09 May 2023 14:44 |
| Last Modified: | 09 May 2023 14:44 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49796 |
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