3EDV

Crystal Structure of Repeats 14-16 of Beta2-Spectrin

3EDV の概要

• エントリーDOI: 10.2210/pdb3edv/pdb
• 分子名称: Spectrin beta chain, brain 1, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: spectrin repeat, coiled coil, actin capping, actin-binding, alternative splicing, calmodulin-binding, cytoplasm, cytoskeleton, glycoprotein, membrane, phosphoprotein, polymorphism, structural protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm, cytoskeleton (By similarity). Isoform 2: Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q01082
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76279.13

構造登録者

Michaely, P.,Tomchick, D.R. (登録日: 2008-09-03, 公開日: 2009-01-20, 最終更新日: 2024-02-21)

主引用文献

Davis, L.,Abdi, K.,Machius, M.,Brautigam, C.,Tomchick, D.R.,Bennett, V.,Michaely, P.
Localization and Structure of the Ankyrin-binding Site on beta2-Spectrin
J.Biol.Chem., 284:6982-6987, 2009

PubMed Abstract: Spectrins are tetrameric actin-cross-linking proteins that form an elastic network, termed the membrane skeleton, on the cytoplasmic surface of cellular membranes. At the plasma membrane, the membrane skeleton provides essential support, preventing loss of membrane material to environmental shear stresses. The skeleton also controls the location, abundance, and activity of membrane proteins that are critical to cell and tissue function. The ability of the skeleton to modulate membrane stability and function requires adaptor proteins that bind the skeleton to membranes. The principal adaptors are the ankyrin proteins, which bind to the beta-subunit of spectrin and to the cytoplasmic domains of numerous integral membrane proteins. Here, we present the crystal structure of the ankyrin-binding domain of human beta2-spectrin at 1.95 A resolution together with mutagenesis data identifying the binding surface for ankyrins on beta2-spectrin.

PubMed: 19098307
DOI: 10.1074/jbc.M809245200

実験手法

X-RAY DIFFRACTION (1.951 Å)