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spinqualitylabelsall models PDB ID 1gg3 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.80Å
Coordinates:	save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF THE PROTEIN 4.1R MEMBRANE BINDING DOMAIN

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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

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