4rlv | pdb_00004rlv

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

spinqualitylabelsall models 4rlv, resolution 3.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rlv is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 NonStd Res: MSE Related: 4rly Gene: Ank1, ANK2 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Structural basis of diverse membrane target recognitions by ankyrins.,Wang C, Wei Z, Chen K, Ye F, Yu C, Bennett V, Zhang M Elife. 2014 Nov 10;3. doi: 10.7554/eLife.04353. PMID:25383926 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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