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1xdx
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(New page: 200px<br /><applet load="1xdx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xdx" /> '''Solution Structure of the Tctex1 Light Chain...)
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Revision as of 23:50, 24 November 2007
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Solution Structure of the Tctex1 Light Chain From Chlamydomonas Inner Dynein Arm I1
Overview
Tctex1 is a light chain found in both cytoplasmic and flagellar dyneins, and is involved in many fundamental cellular activities, including, rhodopsin transport within photoreceptors, and may function in the, non-Mendelian transmission of t haplotypes in mice. Here, we present the, NMR solution structure for the Tctex1 dimer from Chlamydomonas axonemal, inner dynein arm I1. Structural comparisons reveal a strong similarity, with the LC8 dynein light chain dimer, including formation of a, strand-switched beta sheet interface. Analysis of the Tctex1 structure, enables the dynein intermediate chain binding site to be identified and, suggests a mechanism by which cargo proteins might be attached to this, microtubule motor complex. Comparison with the alternate dynein light, chain rp3 reveals how the specificity of dynein-cargo interactions, mediated by these dynein components is achieved. In addition, this, structure provides insight into the consequences of the mutations found in, the t haplotype forms of this protein.
About this Structure
1XDX is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.
Reference
Solution structure of the Tctex1 dimer reveals a mechanism for dynein-cargo interactions., Wu H, Maciejewski MW, Takebe S, King SM, Structure. 2005 Feb;13(2):213-23. PMID:15698565
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