Solution structure of isoform 1 of Roadblock/LC7, a light chain in the dynein complex.
Solution structure of isoform 1 of Roadblock/LC7, a light chain in the dynein complex.
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DOI：
10.1016/j.jmb.2005.10.017
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发表时间：
2005-12
影响因子：
5.6
通讯作者：
Jikui Song;R. Tyler;Min S. Lee;Ejan M. Tyler;J. Markley
中科院分区：
文献类型：
--
作者：
Jikui Song;R. Tyler;Min S. Lee;Ejan M. Tyler;J. Markley
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 β3-strands pair with each other and form a continuous ten-stranded β-sheet. The 25-residue α2-helix from one subunit packs antiparallel to that of the other subunit on the face of the β-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.
