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- W1981361706 abstract "TcTex-1, one of three dynein light chains of the dynein motor complex, has been implicated in targeting and binding cargoes to cytoplasmic dynein for retrograde or apical transport. Interactions between TcTex-1 and a diverse set of proteins such as the dynein intermediate chain, Fyn, DOC2, FIP1, the poliovirus receptor, CD155, and the rhodopsin cytoplasmic tail have been reported; yet, despite the broad range of targets, a consensus binding sequence remains uncertain. Consequently, we have solved the crystal structure of the full-length Drosophila homolog of TcTex-1 to 1.7 A resolution using MAD phasing to gain insight into its function and target specificity. The structure is homodimeric with a domain swapping of β-strand 2 and has a fold similar to the dynein light chain, LC8. Based on structural alignment, the TcTex-1 and LC8 sequences show no identity, although the root mean square deviation between secondary structural elements is less than 1.6 A. Moreover, the N terminus, which is equivalent to β-strand 1 in LC8, is splayed out and binds to a crystallographic dimer as an anti-parallel β-strand at the same position as the neuronal nitric-oxide synthase peptide in the LC8 complex. Similarity to LC8 and comparison to the LC8-neuronal nitricoxide synthase complex suggest that TcTex-1 binds its targets in a similar manner as LC8 and provides insight to the lack of strict sequence identity among the targets for TcTex-1." @default.
- W1981361706 created "2016-06-24" @default.
- W1981361706 creator A5026978349 @default.
- W1981361706 creator A5030659071 @default.
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- W1981361706 date "2005-06-01" @default.
- W1981361706 modified "2023-09-30" @default.
- W1981361706 title "Crystal Structure of Dynein Light Chain TcTex-1" @default.
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- W1981361706 doi "https://doi.org/10.1074/jbc.m414643200" @default.
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