| http://purl.uniprot.org/citations/30224736 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30224736 | http://www.w3.org/2000/01/rdf-schema#comment | "Actin-cross-linking proteins assemble actin filaments into higher-order structures essential for orchestrating cell shape, adhesion, and motility. Missense mutations in the tandem calponin homology domains of their actin-binding domains (ABDs) underlie numerous genetic diseases, but a molecular understanding of these pathologies is hampered by the lack of high-resolution structures of any actin-cross-linking protein bound to F-actin. Here, taking advantage of a high-affinity, disease-associated mutant of the human filamin A (FLNa) ABD, we combine cryo-electron microscopy and functional studies to reveal at near-atomic resolution how the first calponin homology domain (CH1) and residues immediately N-terminal to it engage actin. We further show that reorientation of CH2 relative to CH1 is required to avoid clashes with actin and to expose F-actin-binding residues on CH1. Our data explain localization of disease-associated loss-of-function mutations to FLNaCH1 and gain-of-function mutations to the regulatory FLNaCH2. Sequence conservation argues that this provides a general model for ABD-F-actin binding."xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41594-018-0128-3"xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/author | "Simon B."xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/author | "Calderwood D.A."xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/author | "Baldassarre M."xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/author | "Huet-Calderwood C."xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/author | "Huehn A."xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/author | "Sindelar C.V."xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/author | "Iwamoto D.V."xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/name | "Nat Struct Mol Biol"xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/pages | "918-927"xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/title | "Structural basis of the filamin A actin-binding domain interaction with F-actin."xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://purl.uniprot.org/core/volume | "25"xsd:string |
| http://purl.uniprot.org/citations/30224736 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/30224736 |
| http://purl.uniprot.org/citations/30224736 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/30224736 |
| http://purl.uniprot.org/uniprot/#_P0CU65-mappedCitation-30224736 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/30224736 |
| http://purl.uniprot.org/uniprot/#_P68139-mappedCitation-30224736 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/30224736 |
| http://purl.uniprot.org/uniprot/#_P21333-mappedCitation-30224736 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/30224736 |
| http://purl.uniprot.org/uniprot/P21333 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/30224736 |
| http://purl.uniprot.org/uniprot/P0CU65 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/30224736 |
| http://purl.uniprot.org/uniprot/P68139 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/30224736 |