1n11
From Proteopedia
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D34 REGION OF HUMAN ANKYRIN-R AND LINKER
Contents |
Overview
Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. The N-terminal, 'membrane-binding' domain of ankyrins contains 24 ANK repeats and mediates most binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. Here we report the crystal structure of a human ankyrinR construct containing ANK repeats 13-24 and a portion of the spectrin-binding domain. The ANK repeats are observed to form a contiguous spiral stack with which the spectrin-binding domain fragment associates as an extended strand. The structural information has been used to construct models of all 24 repeats of the membrane-binding domain as well as the interactions of the repeats with the Cl/HCO(3) anion exchanger and clathrin. These models, together with available binding studies, suggest that ion transporters such as the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Disease
Known diseases associated with this structure: Chondrocalcinosis 2 OMIM:[605145], Craniometaphyseal dysplasia OMIM:[605145]
About this Structure
1N11 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a 12 ANK repeat stack from human ankyrinR., Michaely P, Tomchick DR, Machius M, Anderson RG, EMBO J. 2002 Dec 2;21(23):6387-96. PMID:12456646
Page seeded by OCA on Thu Feb 21 14:01:05 2008
Categories: Homo sapiens | Single protein | Anderson, R G.W. | Machius, M. | Michaely, P. | Tomchick, D R. | BR | CL | Anion exchanger | Ankyrin | Band 3 | Clathrin
