1ygt
From Proteopedia
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- | [[Image:1ygt.gif|left|200px]] | + | [[Image:1ygt.gif|left|200px]] |
- | + | ||
- | '''Dynein Light Chain TcTex-1''' | + | {{Structure |
+ | |PDB= 1ygt |SIZE=350|CAPTION= <scene name='initialview01'>1ygt</scene>, resolution 1.7Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= Dlc90F, Tctex ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]) | ||
+ | }} | ||
+ | |||
+ | '''Dynein Light Chain TcTex-1''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1YGT is a [ | + | 1YGT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YGT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15701632 15701632] |
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: domain swapping]] | [[Category: domain swapping]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:22:38 2008'' |
Revision as of 13:22, 20 March 2008
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, resolution 1.7Å | |||||||
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Ligands: | |||||||
Gene: | Dlc90F, Tctex (Drosophila melanogaster) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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 Thu Mar 20 15:22:38 2008