Reference : Two distinct myosin light chain structures are induced by specific variations within ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/15206
Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications
English
Terrak, Mohammed mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Wu, G. [> > > >]
Stafford, W. F. [> > > >]
Lu, R. C. [> > > >]
Dominguez, R. [> > > >]
2003
EMBO Journal
22
3
362-71
Yes (verified by ORBi)
International
0261-4189
[en] Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Crystallography, X-Ray ; Models, Molecular ; Molecular Sequence Data ; Myosin Heavy Chains/chemistry/metabolism ; Myosin Light Chains/*chemistry/metabolism ; Myosin Type V/chemistry/metabolism ; Protein Binding ; *Protein Conformation ; Saccharomyces cerevisiae Proteins/*chemistry/metabolism ; Sequence Alignment ; Support, U.S. Gov't, Non-P.H.S. ; Support, U.S. Gov't, P.H.S.
[en] IQ motifs are widespread in nature. Mlc1p is a calmodulin-like myosin light chain that binds to IQ motifs of a class V myosin, Myo2p, and an IQGAP-related protein, Iqg1p, playing a role in polarized growth and cytokinesis in Saccharomyces cerevisiae. The crystal structures of Mlc1p bound to IQ2 and IQ4 of Myo2p differ dramatically. When bound to IQ2, Mlc1p adopts a compact conformation in which both the N- and C-lobes interact with the IQ motif. However, in the complex with IQ4, the N-lobe no longer interacts with the IQ motif, resulting in an extended conformation of Mlc1p. The two light chain structures relate to two distinct subfamilies of IQ motifs, one of which does not interact with the N-lobes of calmodulin-like light chains. The correlation between light chain structure and IQ sequence is demonstrated further by sedimentation velocity analysis of complexes of Mlc1p with IQ motifs from Myo2p and Iqg1p. The resulting 'free' N-lobes of myosin light chains in the extended conformation could mediate the formation of ternary complexes during protein localization and/or partner recruitment.
http://hdl.handle.net/2268/15206

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Restricted access
MLC1 EMBO.pdfNo commentaryPublisher postprint404.64 kBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.