Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 354, Issue 5, Pages 1043-1051Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2005.10.017
Keywords
dynein light chain; Roadblock LC/7; IC74-1 fragment; protein-protein interaction; three-dimensional solution structure
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Funding
- NCRR NIH HHS [P41 RR02301] Funding Source: Medline
- NIGMS NIH HHS [P50 GM64598, P41 GM66326] Funding Source: Medline
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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 I 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 beta(3)-strands pair with each other and form a continuous ten-stranded beta-sheet. The 25-residue alpha(2)-helix from one subunit packs antiparallel to that of the other subunit on the face of the P-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. (c) 2005 Elsevier Ltd. All rights reserved.
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