8chh | pdb_00008chh

SH3 domain solved by the exact solid-state method from the Bruker Dynamics Center using the correction method for spin-diffusion with PDB 2NUZ as reference

spinqualitylabelsall models 8chh Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8chh 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. 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. Publication Abstract from PubMed Understanding macromolecular function, interactions, and stability hinges on detailed assessment of conformational ensembles. For solid proteins, accurate elucidation of the spatial aspects of dynamics at physiological temperatures is limited by the qualitative character or low abundance of solid-state nuclear magnetic resonance internuclear distance information. Here, we demonstrate access to abundant proton-proton internuclear distances for integrated structural biology and chemistry with unprecedented accuracy. Apart from highest-resolution single-state structures, the exact distances enable molecular dynamics (MD) ensemble simulations orchestrated by a dense network of experimental interproton distance boundaries gathered in the context of their physical lattices. This direct embedding of experimental ensemble distances into MD will provide access to representative, atomic-level spatial details of conformational dynamics in supramolecular assemblies, crystalline and lipid-embedded proteins, and beyond. Integrated Assessment of the Structure and Dynamics of Solid Proteins.,Soldner B, Grohe K, Neidig P, Auch J, Blach S, Klein A, Vasa SK, Schafer LV, Linser R J Phys Chem Lett. 2023 Feb 23;14(7):1725-1731. doi: 10.1021/acs.jpclett.2c03398. , Epub 2023 Feb 9. PMID:36757335 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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