4jhd
From Proteopedia
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- | + | {{STRUCTURE_4jhd| PDB=4jhd | SCENE= }} | |
+ | ===Crystal Structure of an Actin Dimer in Complex with the Actin Nucleator Cordon-Bleu=== | ||
+ | {{ABSTRACT_PUBMED_23727244}} | ||
- | + | ==Function== | |
+ | [[http://www.uniprot.org/uniprot/ACT1_DROME ACT1_DROME]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. [[http://www.uniprot.org/uniprot/COBL_MOUSE COBL_MOUSE]] Plays an important role in the reorganization of the actin cytoskeleton. Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. Regulates neuron morphogenesis and increases branching of axons and dendrites. Regulates dendrite branching in Purkinje cells.<ref>PMID:17956734</ref> <ref>PMID:23223303</ref> | ||
- | + | ==About this Structure== | |
+ | [[4jhd]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JHD OCA]. | ||
- | + | ==Reference== | |
+ | <ref group="xtra">PMID:023727244</ref><references group="xtra"/><references/> | ||
+ | [[Category: Drosophila melanogaster]] | ||
+ | [[Category: Mus musculus]] | ||
+ | [[Category: Chen, X.]] | ||
+ | [[Category: Ni, F.]] | ||
+ | [[Category: Wang, Q.]] | ||
+ | [[Category: Actin cytoskeleton]] | ||
+ | [[Category: Actin filament nucleator]] | ||
+ | [[Category: Nuclear actin]] | ||
+ | [[Category: Nucleation]] | ||
+ | [[Category: Structural protein-protein binding complex]] | ||
+ | [[Category: Tandem w domain]] |
Revision as of 17:58, 19 June 2013
Contents |
Crystal Structure of an Actin Dimer in Complex with the Actin Nucleator Cordon-Bleu
Template:ABSTRACT PUBMED 23727244
Function
[ACT1_DROME] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. [COBL_MOUSE] Plays an important role in the reorganization of the actin cytoskeleton. Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling three actin monomers in cross-filament orientation and thereby promotes growth of actin filaments at the barbed end. Can also mediate actin depolymerization at barbed ends and severing of actin filaments. Promotes formation of cell ruffles. Regulates neuron morphogenesis and increases branching of axons and dendrites. Regulates dendrite branching in Purkinje cells.[1] [2]
About this Structure
4jhd is a 6 chain structure with sequence from Drosophila melanogaster and Mus musculus. Full crystallographic information is available from OCA.
Reference
- Chen X, Ni F, Tian X, Kondrashkina E, Wang Q, Ma J. Structural Basis of Actin Filament Nucleation by Tandem W Domains. Cell Rep. 2013 May 29. pii: S2211-1247(13)00210-6. doi:, 10.1016/j.celrep.2013.04.028. PMID:23727244 doi:10.1016/j.celrep.2013.04.028
- ↑ Ahuja R, Pinyol R, Reichenbach N, Custer L, Klingensmith J, Kessels MM, Qualmann B. Cordon-bleu is an actin nucleation factor and controls neuronal morphology. Cell. 2007 Oct 19;131(2):337-50. PMID:17956734 doi:10.1016/j.cell.2007.08.030
- ↑ Haag N, Schwintzer L, Ahuja R, Koch N, Grimm J, Heuer H, Qualmann B, Kessels MM. The actin nucleator Cobl is crucial for Purkinje cell development and works in close conjunction with the F-actin binding protein Abp1. J Neurosci. 2012 Dec 5;32(49):17842-56. doi: 10.1523/JNEUROSCI.0843-12.2012. PMID:23223303 doi:10.1523/JNEUROSCI.0843-12.2012