1nr0
From Proteopedia
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'''Two Seven-Bladed Beta-Propeller Domains Revealed By The Structure Of A C. elegans Homologue Of Yeast Actin Interacting Protein 1 (AIP1).''' | '''Two Seven-Bladed Beta-Propeller Domains Revealed By The Structure Of A C. elegans Homologue Of Yeast Actin Interacting Protein 1 (AIP1).''' | ||
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[[Category: Ono, S.]] | [[Category: Ono, S.]] | ||
[[Category: Vorobiev, S M.]] | [[Category: Vorobiev, S M.]] | ||
| - | [[Category: | + | [[Category: Actin interacting protein]] |
| - | [[Category: | + | [[Category: Adf]] |
| - | [[Category: | + | [[Category: Beta propeller]] |
| - | [[Category: | + | [[Category: Cofilin]] |
| - | [[Category: | + | [[Category: New york structural genomix research consortium]] |
| - | [[Category: | + | [[Category: Nysgxrc]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Wd40 repeat]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:52:45 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:52, 2 May 2008
Two Seven-Bladed Beta-Propeller Domains Revealed By The Structure Of A C. elegans Homologue Of Yeast Actin Interacting Protein 1 (AIP1).
Overview
Actin-interacting protein 1 (AIP1) is a WD40 repeat protein that enhances actin filament disassembly in the presence of actin-depolymerizing factor (ADF)/cofilin. AIP1 also caps the barbed end of ADF/cofilin-bound actin filament. However, the mechanism by which AIP1 interacts with ADF/cofilin and actin is not clearly understood. We determined the crystal structure of Caenorhabditis elegans AIP1 (UNC-78), which revealed 14 WD40 modules arranged in two seven-bladed beta-propeller domains. The structure allowed for the mapping of conserved surface residues, and mutagenesis studies identified five residues that affected the ADF/cofilin-dependent actin filament disassembly activity. Mutations of these residues, which reside in blades 3 and 4 in the N-terminal propeller domain, had significant effects on the disassembly activity but did not alter the barbed end capping activity. These data support a model in which this conserved surface of AIP1 plays a direct role in enhancing fragmentation/depolymerization of ADF/cofilin-bound actin filaments but not in barbed end capping.
About this Structure
1NR0 is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
Identification of functional residues on Caenorhabditis elegans actin-interacting protein 1 (UNC-78) for disassembly of actin depolymerizing factor/cofilin-bound actin filaments., Mohri K, Vorobiev S, Fedorov AA, Almo SC, Ono S, J Biol Chem. 2004 Jul 23;279(30):31697-707. Epub 2004 May 18. PMID:15150269 Page seeded by OCA on Sat May 3 02:52:45 2008
Categories: Caenorhabditis elegans | Single protein | Almo, S C. | Burley, S K. | Mohri, K. | NYSGXRC, New York Structural GenomiX Research Consortium. | Ono, S. | Vorobiev, S M. | Actin interacting protein | Adf | Beta propeller | Cofilin | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomic | Wd40 repeat
