3EDV

Crystal Structure of Repeats 14-16 of Beta2-Spectrin

Summary for 3EDV

• Entry DOI: 10.2210/pdb3edv/pdb
• Descriptor: Spectrin beta chain, brain 1, MAGNESIUM ION (3 entities in total)
• Functional Keywords: spectrin repeat, coiled coil, actin capping, actin-binding, alternative splicing, calmodulin-binding, cytoplasm, cytoskeleton, glycoprotein, membrane, phosphoprotein, polymorphism, structural protein
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm, cytoskeleton (By similarity). Isoform 2: Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q01082
• Total number of polymer chains: 2
• Total formula weight: 76279.13

Authors

Michaely, P.,Tomchick, D.R. (deposition date: 2008-09-03, release date: 2009-01-20, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.951 Å)