3sjh | pdb_00003sjh

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

Function

[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

About this Structure

3sjh is a 2 chain structure with sequence from 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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

3sjh | pdb_00003sjh

Contents

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

Function

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools