4RLV

Crystal Structure of AnkB 24 Ankyrin Repeats in Complex with AnkR Autoinhibition Segment

Summary for 4RLV

• Entry DOI: 10.2210/pdb4rlv/pdb
• Related: 4RLY
• Descriptor: Ankyrin-1, Ankyrin-2, SULFATE ION (2 entities in total)
• Functional Keywords: ank repeat, protein-protein interaction, structural protein
• Biological source: Mus musculus (mouse, human); More
• Cellular location: Cytoplasm, cytoskeleton : Q01484
• Total number of polymer chains: 1
• Total formula weight: 98876.09

Authors

Wei, Z.,Wang, C.,Zhang, M. (deposition date: 2014-10-18, release date: 2014-11-26, Last modification date: 2024-11-27)

Primary citation

Wang, C.,Wei, Z.,Chen, K.,Ye, F.,Yu, C.,Bennett, V.,Zhang, M.
Structural basis of diverse membrane target recognitions by ankyrins.
Elife, 3:e04353-, 2014

PubMed Abstract: Ankyrin adaptors together with their spectrin partners coordinate diverse ion channels and cell adhesion molecules within plasma membrane domains and thereby promote physiological activities including fast signaling in the heart and nervous system. Ankyrins specifically bind to numerous membrane targets through their 24 ankyrin repeats (ANK repeats), although the mechanism for the facile and independent evolution of these interactions has not been resolved. Here we report the structures of ANK repeats in complex with an inhibitory segment from the C-terminal regulatory domain and with a sodium channel Nav1.2 peptide, respectively, showing that the extended, extremely conserved inner groove spanning the entire ANK repeat solenoid contains multiple target binding sites capable of accommodating target proteins with very diverse sequences via combinatorial usage of these sites. These structures establish a framework for understanding the evolution of ankyrins' membrane targets, with implications for other proteins containing extended ANK repeat domains.

PubMed: 25383926
DOI: 10.7554/eLife.04353

Experimental method

X-RAY DIFFRACTION (3.4945 Å)