4bw8 | pdb_00004bw8

Calmodulin with small bend in central helix

spinqualitylabelsall models 4bw8, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bw8 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Related: 4bw7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Calmodulin is one of the most well characterized proteins and a widely used model system for calcium binding and large-scale protein conformational changes. Its long central helix is usually cut in half when a target peptide is bound. Here, two new crystal structures of calmodulin are presented, in which conformations possibly representing the first steps of calmodulin conformational collapse have been trapped. The central helix in the two structures is bent in the middle, causing a significant movement of the N- and C-terminal lobes with respect to one another. In both of the bent structures, a nearby polar side chain is inserted into the helical groove, disrupting backbone hydrogen bonding. The structures give an insight into the details of the factors that may be involved in the distortion of the central helix upon ligand peptide binding. Crystallographic snapshots of initial steps in the collapse of the calmodulin central helix.,Kursula P Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):24-30. doi:, 10.1107/S1399004713024437. Epub 2013 Dec 24. PMID:24419375 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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