3sjh
From Proteopedia
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+ | {{STRUCTURE_3sjh| PDB=3sjh | SCENE= }} | ||
- | + | ===Crystal Structure of a chimera containing the N-terminal domain (residues 8-29) of drosophila Ciboulot and the C-terminal domain (residues 18-44) of bovine Thymosin-beta4, bound to G-actin-ATP-Latrunculin A=== | |
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+ | The line below this paragraph, {{ABSTRACT_PUBMED_22193718}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 22193718 is the PubMed ID number. | ||
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+ | {{ABSTRACT_PUBMED_22193718}} | ||
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+ | ==About this Structure== | ||
+ | [[3sjh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster,_bos_taurus Drosophila melanogaster, bos taurus] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SJH OCA]. | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:022193718</ref><references group="xtra"/> | ||
+ | [[Category: Drosophila melanogaster, bos taurus]] | ||
+ | [[Category: Oryctolagus cuniculus]] | ||
+ | [[Category: Carlier, M F.]] | ||
+ | [[Category: Didry, D.]] | ||
+ | [[Category: Husson, C.]] | ||
+ | [[Category: Renault, L.]] | ||
+ | [[Category: Contractile protein]] | ||
+ | [[Category: Protein binding]] | ||
+ | [[Category: Protein-protein complex]] |
Revision as of 06:31, 25 January 2012
Crystal Structure of a chimera containing the N-terminal domain (residues 8-29) of drosophila Ciboulot and the C-terminal domain (residues 18-44) of bovine Thymosin-beta4, bound to G-actin-ATP-Latrunculin A
Template:ABSTRACT PUBMED 22193718
About this Structure
3sjh is a 2 chain structure with sequence from Drosophila melanogaster, bos taurus and Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
- Didry D, Cantrelle FX, Husson C, Roblin P, Moorthy AM, Perez J, Le Clainche C, Hertzog M, Guittet E, Carlier MF, van Heijenoort C, Renault L. How a single residue in individual beta-thymosin/WH2 domains controls their functions in actin assembly. EMBO J. 2011 Dec 23. doi: 10.1038/emboj.2011.461. PMID:22193718 doi:10.1038/emboj.2011.461