Yasunaga, Mai, Ipsaro, Jonathan J., Mondragón, Alfonso (April 2012) Structurally Similar but Functionally Diverse ZU5 Domains in Human Erythrocyte Ankyrin. Journal of Molecular Biology, 417 (4). pp. 336-350. ISSN 0022-2836
Abstract
The metazoan cell membrane is highly organized. Maintaining such organization and preserving membrane integrity under different conditions are accomplished through intracellular tethering to an extensive, flexible protein network. Spectrin, the principal component of this network, is attached to the membrane through the adaptor protein ankyrin, which directly bridges the interaction between β-spectrin and membrane proteins. Ankyrins have a modular structure that includes two tandem ZU5 domains. The first domain, ZU5A, is directly responsible for binding β-spectrin. Here, we present a structure of the tandem ZU5 repeats of human erythrocyte ankyrin. Structural and biophysical experiments show that the second ZU5 domain, ZU5B, does not participate in spectrin binding. ZU5B is structurally similar to the ZU5 domain found in the netrin receptor UNC5b supramodule, suggesting that it could interact with other domains in ankyrin. Comparison of several ZU5 domains demonstrates that the ZU5 domain represents a compact and versatile protein interaction module.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | protein–protein interactions protein structure ankyrin-R UNC5b crystallography |
| Subjects: | bioinformatics bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering |
| CSHL Authors: | |
| Communities: | CSHL Post Doctoral Fellows CSHL labs > Joshua-Tor lab |
| Depositing User: | Matt Covey |
| Date: | 6 April 2012 |
| Date Deposited: | 17 Jan 2013 21:01 |
| Last Modified: | 20 Jul 2021 14:52 |
| PMCID: | PMC3312341 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/27089 |
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