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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MYOC_DICDI MYOC_DICDI]] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Involved in the process of phagocytosis and appears to support streaming behavior.<ref>PMID:8609164</ref> | [[http://www.uniprot.org/uniprot/MYOC_DICDI MYOC_DICDI]] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Involved in the process of phagocytosis and appears to support streaming behavior.<ref>PMID:8609164</ref> | ||
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== Publication Abstract from PubMed == | |||
Myosin light chains are key regulators of class 1 myosins and typically comprise two domains, with calmodulin being the archetypal example. They bind IQ motifs within the myosin neck region and amplify conformational changes in motor domain. A single lobe light chain, myosin light chain C (MlcC), was recently identified and shown to specifically bind to two sequentially divergent IQ motifs of the Dictyostelium myosin-1C. Towards providing a molecular basis of this interaction, the structures of apo-MlcC and a 2:1 MlcC:myosin-1C neck complex were determined. The two non-functional EF-hand motifs of MlcC pack together to form a globular four-helix bundle that opens up to expose a central hydrophobic groove, which interacts the N-terminal portion of the divergent IQ1 and IQ2 motifs. N- and C-terminal regions of MlcC make critical contacts that contribute to its specific interactions with the myosin-1C divergent IQ motifs; contacts that deviate from the traditional mode of calmodulin-IQ recognition. | |||
Structure of the single-lobe myosin light chain C in complex with the light chain-binding domains of myosin-1C provides insights into divergent IQ-motif recognition.,Langelaan DN, Liburd J, Yang Y, Miller E, Chitayat S, Crawley SW, Cote GP, Smith SP J Biol Chem. 2016 Jul 27. pii: jbc.M116.746313. PMID:27466369<ref>PMID:27466369</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | == References == | ||
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Revision as of 11:12, 10 August 2016
Complex of MlcC bound to the tandem IQ motif of MyoCComplex of MlcC bound to the tandem IQ motif of MyoC
Structural highlights
Function[MYOC_DICDI] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. Involved in the process of phagocytosis and appears to support streaming behavior.[1] Publication Abstract from PubMedMyosin light chains are key regulators of class 1 myosins and typically comprise two domains, with calmodulin being the archetypal example. They bind IQ motifs within the myosin neck region and amplify conformational changes in motor domain. A single lobe light chain, myosin light chain C (MlcC), was recently identified and shown to specifically bind to two sequentially divergent IQ motifs of the Dictyostelium myosin-1C. Towards providing a molecular basis of this interaction, the structures of apo-MlcC and a 2:1 MlcC:myosin-1C neck complex were determined. The two non-functional EF-hand motifs of MlcC pack together to form a globular four-helix bundle that opens up to expose a central hydrophobic groove, which interacts the N-terminal portion of the divergent IQ1 and IQ2 motifs. N- and C-terminal regions of MlcC make critical contacts that contribute to its specific interactions with the myosin-1C divergent IQ motifs; contacts that deviate from the traditional mode of calmodulin-IQ recognition. Structure of the single-lobe myosin light chain C in complex with the light chain-binding domains of myosin-1C provides insights into divergent IQ-motif recognition.,Langelaan DN, Liburd J, Yang Y, Miller E, Chitayat S, Crawley SW, Cote GP, Smith SP J Biol Chem. 2016 Jul 27. pii: jbc.M116.746313. PMID:27466369[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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