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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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'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XDX OCA].
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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]]
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[[Category: King, S.M.]]
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[[Category: King, S M.]]
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[[Category: Maciejewski, M.W.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:57:37 2007''
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''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


1xdx

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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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