6fsa | pdb_00006fsa

Beta-Cardiac myosin post-rigor

spinqualitylabelsall models 6fsa, resolution 2.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fsa is a 4 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, EDO, FMT, MG NonStd Res: MLY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MYH7_BOVIN] Muscle contraction. [MYL3_BOVIN] Regulatory light chain of myosin. Does not bind calcium. Publication Abstract from PubMed Hypertrophic cardiomyopathies (HCM) result from distinct single-point mutations in sarcomeric proteins that lead to muscle hypercontractility. While different models account for a pathological increase in the power output, clear understanding of the molecular basis of dysfunction in HCM is the mandatory next step to improve current treatments. Here, we present an optimized quasi-atomic model of the sequestered state of cardiac myosin coupled to X-ray crystallography and in silico analysis of the mechanical compliance of the lever arm, allowing the systematic study of a large set of HCM mutations and the definition of different mutation classes based on their effects on lever arm compliance, sequestered state stability, and motor functions. The present work reconciles previous models and explains how distinct HCM mutations can have disparate effects on the motor mechano-chemical parameters and yet lead to the same disease. The framework presented here can guide future investigations aiming at finding HCM treatments. Hypertrophic cardiomyopathy disease results from disparate impairments of cardiac myosin function and auto-inhibition.,Robert-Paganin J, Auguin D, Houdusse A Nat Commun. 2018 Oct 1;9(1):4019. doi: 10.1038/s41467-018-06191-4. PMID:30275503 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myosin

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