Structurally Similar but Functionally Diverse ZU5 Domains in Human Erythrocyte Ankyrin

Journal Article · Thu Oct 02 04:00:00 EDT 2014 · J. Mol. Biol.

DOI:https://doi.org/10.1016/j.jmb.2012.01.041· OSTI ID:1038295

Yasunaga, Mai; Ipsaro, Jonathan J.; Mondragón, Alfonso ^[1]

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1. NWU

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 {beta}-spectrin and membrane proteins. Ankyrins have a modular structure that includes two tandem ZU5 domains. The first domain, ZU5A, is directly responsible for binding {beta}-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.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: UNIVERSITYNIHOTHER U.S. STATES
• OSTI ID: 1038295
• Journal Information: J. Mol. Biol., Journal Name: J. Mol. Biol. Journal Issue: (6) ; 04, 2012 Vol. 417; ISSN JMOBAK; ISSN 0022-2836
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
CELL MEMBRANES
ERYTHROCYTES
MEMBRANE PROTEINS
MEMBRANES
MODULAR STRUCTURES
PROTEINS