1ygt

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[[Image:1ygt.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1ygt", creates the "Structure Box" on the page.
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|GENE= Dlc90F, Tctex ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ygt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ygt OCA], [http://www.ebi.ac.uk/pdbsum/1ygt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ygt RCSB]</span>
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'''Dynein Light Chain TcTex-1'''
'''Dynein Light Chain TcTex-1'''
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[[Category: Williams, J C.]]
[[Category: Williams, J C.]]
[[Category: Xie, H.]]
[[Category: Xie, H.]]
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[[Category: domain swapping]]
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[[Category: Domain swapping]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:17:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:06:47 2008''
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Revision as of 13:18, 3 May 2008

Template:STRUCTURE 1ygt

Dynein Light Chain TcTex-1


Overview

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 beta-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 beta-strand 1 in LC8, is splayed out and binds to a crystallographic dimer as an anti-parallel beta-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.

About this Structure

1YGT is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Crystal structure of dynein light chain TcTex-1., Williams JC, Xie H, Hendrickson WA, J Biol Chem. 2005 Jun 10;280(23):21981-6. Epub 2005 Feb 8. PMID:15701632 Page seeded by OCA on Sat May 3 16:17:59 2008

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