| http://purl.uniprot.org/citations/17251352 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17251352 | http://www.w3.org/2000/01/rdf-schema#comment | "Actin-related protein (Arp) 2/3 complex nucleates new branches in actin filaments playing a key role in controlling eukaryotic cell motility. This process is tightly regulated by activating factors: ATP and WASp-family proteins. However, the mechanism of activation remains largely hypothetical. We used radiolytic protein footprinting with mass spectrometry in solution to probe the effects of nucleotide- and WASp-binding on Arp2/3. These results represent two significant advances in such footprinting approaches. First, Arp2/3 is the most complex macromolecular assembly yet examined; second, only a few picomoles of Arp2/3 was required for individual experiments. In terms of structural biology of Arp 2/3, we find that ATP binding induces conformational changes within Arp2/3 complex in Arp3 (localized in peptide segments 5-18, 212-225, and 318-327) and Arp2 (within peptide segment 300-316). These data are consistent with nucleotide docking within the nucleotide clefts of the actin-related proteins promoting closure of the cleft of the Arp3 subunit. However, ATP binding does not induce conformational changes in the other Arp subunits. Arp2/3 complex binds to WASp within the C subdomain at residue Met 474 and within the A subdomain to Trp 500. Our data suggest a bivalent attachment of WASp to Arp3 (within peptides 162-191 and 318-329) and Arp2 (within peptides 66-80 and 87-97). WASp-dependent protections from oxidation within peptides 54-65 and 80-91 of Arp3 and in peptides 300-316 of Arp2 suggest domain rearrangements of Arp2 and Arp3 resulting in a closed conformational state consistent with an "actin-dimer" model for the active state."xsd:string |
| http://purl.uniprot.org/citations/17251352 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0605380104"xsd:string |
| http://purl.uniprot.org/citations/17251352 | http://purl.uniprot.org/core/author | "Almo S.C."xsd:string |
| http://purl.uniprot.org/citations/17251352 | http://purl.uniprot.org/core/author | "Pollard T.D."xsd:string |
| http://purl.uniprot.org/citations/17251352 | http://purl.uniprot.org/core/author | "Chance M.R."xsd:string |
| http://purl.uniprot.org/citations/17251352 | http://purl.uniprot.org/core/author | "Kiselar J.G."xsd:string |
| http://purl.uniprot.org/citations/17251352 | http://purl.uniprot.org/core/author | "Mahaffy R."xsd:string |
| http://purl.uniprot.org/citations/17251352 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17251352 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
| http://purl.uniprot.org/citations/17251352 | http://purl.uniprot.org/core/pages | "1552-1557"xsd:string |
| http://purl.uniprot.org/citations/17251352 | http://purl.uniprot.org/core/title | "Visualizing Arp2/3 complex activation mediated by binding of ATP and WASp using structural mass spectrometry."xsd:string |
| http://purl.uniprot.org/citations/17251352 | http://purl.uniprot.org/core/volume | "104"xsd:string |
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