2z6e

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{{STRUCTURE_2z6e| PDB=2z6e | SCENE= }}
{{STRUCTURE_2z6e| PDB=2z6e | SCENE= }}
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'''Crystal Structure of Human DAAM1 FH2'''
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===Crystal Structure of Human DAAM1 FH2===
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==Overview==
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Reorganization of the actin filament is an essential process for cell motility, cell-cell attachment and intracellular transport. Formin proteins promote nucleation and elongation of the actin filament, and thus are key regulators for this process. The formin homology 2 (FH2) domain forms a head-to-tail ring-shaped dimer, and processively moves towards the barbed end. Dishevelled-associated activator of morphogenesis (DAAM) is a Rho-regulated formin implicated in neuronal development. Here, we present the crystal structure of human DAAM1 FH2 dimer at 2.8 A resolution. This is the first dimeric structure of the mammalian formin. The core structure of human DAAM1 is similar to those of mouse mDia1 and yeast Bni1p, whereas the orientations of the FH2 dimeric rings are different between human DAAM1 and yeast Bni1p, despite their similar dimer interactions. This difference supports the previous prediction that the dimer architecture of the formin is highly flexible in the actin-free state. The results of the actin assembly assays using the DAAM1 mutants demonstrated that the length of the linker connecting the N-terminal domain and the core region is crucial for the activity.
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{{ABSTRACT_PUBMED_17986009}}
==About this Structure==
==About this Structure==
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[[Category: Cytoplasm]]
[[Category: Cytoplasm]]
[[Category: Protein fibril regulator]]
[[Category: Protein fibril regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:17:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:13:50 2008''

Revision as of 05:13, 29 July 2008

Template:STRUCTURE 2z6e

Crystal Structure of Human DAAM1 FH2

Template:ABSTRACT PUBMED 17986009

About this Structure

2Z6E is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human DAAM1 formin homology 2 domain., Yamashita M, Higashi T, Suetsugu S, Sato Y, Ikeda T, Shirakawa R, Kita T, Takenawa T, Horiuchi H, Fukai S, Nureki O, Genes Cells. 2007 Nov;12(11):1255-65. PMID:17986009

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