1gg3
From Proteopedia
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CRYSTAL STRUCTURE OF THE PROTEIN 4.1R MEMBRANE BINDING DOMAIN
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Overview
The crystal structure of the core domain (N-terminal 30 kDa domain) of, cytoskeletal protein 4.1R has been determined and shows a cloverleaf-like, architecture. Each lobe of the cloverleaf contains a specific binding site, for either band 3, glycophorin C/D or p55. At a central region of the, molecule near where the three lobes are joined are two separate calmodulin, (CaM) binding regions. One of these is composed primarily of an, alpha-helix and is Ca 2+ insensitive; the other takes the form of an, extended structure and its binding with CaM is dramatically enhanced by, the presence of Ca 2+, resulting in the weakening of protein 4.1R binding, to its target proteins. This novel architecture, in which the three lobes, bind with three membrane associated proteins, and the location of, calmodulin binding sites provide insight into how the protein 4.1R core, domain interacts with membrane proteins and dynamically regulates cell, shape in response to changes in intracellular Ca2+ levels.
Disease
Known disease associated with this structure: Elliptocytosis-1 OMIM:[130500]
About this Structure
1GG3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization., Han BG, Nunomura W, Takakuwa Y, Mohandas N, Jap BK, Nat Struct Biol. 2000 Oct;7(10):871-5. PMID:11017195
Page seeded by OCA on Mon Nov 12 17:04:52 2007
Categories: Homo sapiens | Single protein | Han, B.G. | 30kd | 4.1r | Blood | Calmodulin | Membrane | N-terminal domain
