1gg3

CRYSTAL STRUCTURE OF THE PROTEIN 4.1R MEMBRANE BINDING DOMAIN

spinqualitylabelsall models 1gg3, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gg3 is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1ef1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [41_HUMAN] Defects in EPB41 are the cause of elliptocytosis type 1 (EL1) [MIM:611804]. EL1 is a Rhesus-linked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant, hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape. Defects in EPB41 are a cause of hereditary pyropoikilocytosis (HPP) [MIM:266140]. HPP is an autosomal recessive hematologic disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells. Function [41_HUMAN] Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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