1y4o
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(New page: 200px<br /><applet load="1y4o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y4o" /> '''Solution structure of a mouse cytoplasmic Ro...)
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Revision as of 04:26, 21 November 2007
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Solution structure of a mouse cytoplasmic Roadblock/LC7 dynein light chain
Overview
Roadblock/LC7 is a member of a class of dynein light chains involved in, regulating the function of the dynein complex. We have determined the, three-dimensional structure of isoform 1 of the mouse Roadblock/LC7, cytoplasmic dynein light chain (robl1_mouse) by NMR spectroscopy. In, contrast to a previously reported NMR structure of the human homolog with, 96% sequence identity (PDB 1TGQ), which showed the protein as a monomer, our results indicate clearly that robl1 exists as a symmetric homodimer., The two beta3-strands pair with each other and form a continuous, ten-stranded beta-sheet. The 25-residue alpha2-helix from one subunit, packs antiparallel to that of the other subunit on the face of the, beta-sheet. Zipper-like hydrophobic contacts between the two helices serve, to stabilize the dimer. Through an NMR titration experiment, we localized, the site on robl1_mouse that interacts with the 40 residue peptide, spanning residues 243 through 282 of IC74-1_rat. These results provide, physical evidence for a symmetrical interaction between dimeric robl1 and, the two molecules of IC74-1 in the dynein complex.
About this Structure
1Y4O is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Solution structure of isoform 1 of Roadblock/LC7, a light chain in the dynein complex., Song J, Tyler RC, Lee MS, Tyler EM, Markley JL, J Mol Biol. 2005 Dec 16;354(5):1043-51. Epub 2005 Nov 2. PMID:16289575
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