1m8m

SOLID-STATE MAS NMR STRUCTURE OF THE A-SPECTRIN SH3 DOMAINSOLID-STATE MAS NMR STRUCTURE OF THE A-SPECTRIN SH3 DOMAIN

Structural highlights 1m8m is a 1 chain structure with sequence from Gallus gallus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solid-state NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SPTN1_CHICK Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization. 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 determination of a representative set of protein structures is a chief aim in structural genomics. Solid-state NMR may have a crucial role in structural investigations of those proteins that do not easily form crystals or are not accessible to solution NMR, such as amyloid systems or membrane proteins. Here we present a protein structure determined by solid-state magic-angle-spinning (MAS) NMR. Almost complete (13)C and (15)N resonance assignments for a micro-crystalline preparation of the alpha-spectrin Src-homology 3 (SH3) domain formed the basis for the extraction of a set of distance restraints. These restraints were derived from proton-driven spin diffusion (PDSD) spectra of biosynthetically site-directed, labelled samples obtained from bacteria grown using [1,3-(13)C]glycerol or [2-(13)C]glycerol as carbon sources. This allowed the observation of long-range distance correlations up to approximately 7 A. The calculated global fold of the alpha-spectrin SH3 domain is based on 286 inter-residue (13)C-(13)C and six (15)N-(15)N restraints, all self-consistently obtained by solid-state MAS NMR. This MAS NMR procedure should be widely applicable to small membrane proteins that can be expressed in bacteria. Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy.,Castellani F, van Rossum B, Diehl A, Schubert M, Rehbein K, Oschkinat H Nature. 2002 Nov 7;420(6911):98-102. PMID:12422222 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Spectrin 3D structures

spinqualitylabelsall models 1m8m Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image