1xdx
From Proteopedia
(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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'''Solution Structure of the Tctex1 Light Chain From Chlamydomonas Inner Dynein Arm I1'''<br /> | '''Solution Structure of the Tctex1 Light Chain From Chlamydomonas Inner Dynein Arm I1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tctex1 is a light chain found in both cytoplasmic and flagellar dyneins | + | 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== | ==About this Structure== | ||
| - | 1XDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http:// | + | 1XDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XDX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chlamydomonas reinhardtii]] | [[Category: Chlamydomonas reinhardtii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: King, S | + | [[Category: King, S M.]] |
| - | [[Category: Maciejewski, M | + | [[Category: Maciejewski, M W.]] |
[[Category: Takebe, S.]] | [[Category: Takebe, S.]] | ||
[[Category: Wu, H.]] | [[Category: Wu, H.]] | ||
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[[Category: tctex1 dimer]] | [[Category: tctex1 dimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:53:47 2008'' |
Revision as of 13:53, 21 February 2008
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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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