2m8u: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
==Solution structure of the Dictyostelium discodieum Myosin Light Chain, MlcC==
==Solution structure of the Dictyostelium discodieum Myosin Light Chain, MlcC==
<StructureSection load='2m8u' size='340' side='right' caption='[[2m8u]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2m8u' size='340' side='right' caption='[[2m8u]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2m8u]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M8U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M8U FirstGlance]. <br>
<table><tr><td colspan='2'>[[2m8u]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M8U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M8U FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2m8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m8u OCA], [http://pdbe.org/2m8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m8u RCSB], [http://www.ebi.ac.uk/pdbsum/2m8u PDBsum]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2m8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m8u OCA], [http://pdbe.org/2m8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m8u RCSB], [http://www.ebi.ac.uk/pdbsum/2m8u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2m8u ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2m8u" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 10:53, 10 August 2016

Solution structure of the Dictyostelium discodieum Myosin Light Chain, MlcCSolution structure of the Dictyostelium discodieum Myosin Light Chain, MlcC

Structural highlights

2m8u is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Langelaan DN, Liburd J, Yang Y, Miller E, Chitayat S, Crawley SW, Cote GP, Smith SP. 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. J Biol Chem. 2016 Jul 27. pii: jbc.M116.746313. PMID:27466369 doi:http://dx.doi.org/10.1074/jbc.M116.746313
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA