| http://purl.uniprot.org/citations/12460563 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12460563 | http://www.w3.org/2000/01/rdf-schema#comment | "IkappaBalpha inhibits transcription factor NF-kappaB activity by specific binding to NF-kappaB heterodimers composed of p65 and p50 subunits. It binds with slightly lower affinity to p65 homodimers and with significantly lower affinity to homodimers of p50. We have employed a structure-based mutagenesis approach coupled with protein-protein interaction assays to determine the source of this dimer selectivity exhibited by IkappaBalpha. Mutation of amino acid residues in IkappaBalpha that contact NF-kappaB only marginally affects complex binding affinity, indicating a lack of hot spots in NF-kappaB/IkappaBalpha complex formation. Conversion of the weak binding NF-kappaB p50 homodimer into a high affinity binding partner of IkappaBalpha requires transfer of both the NLS polypeptide and amino acid residues Asn202 and Ser203 from the NF-kappaB p65 subunit. Involvement of Asn202 and Ser203 in complex formation is surprising as these amino acid residues occupy solvent exposed positions at a distance of 20A from IkappaBalpha in the crystal structures. However, the same amino acid residue positions have been genetically isolated as determinants of binding specificity in a homologous system in Drosophila. X-ray crystallographic and solvent accessibility experiments suggest that these solvent-exposed amino acid residues contribute to NF-kappaB/IkappaBalpha complex formation by modulating the NF-kappaB p65 subunit NLS polypeptide."xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0022-2836(02)01149-x"xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/author | "Komives E.A."xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/author | "Ghosh G."xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/author | "Hughes C.A."xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/author | "Reeves R."xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/author | "Huang D.B."xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/author | "Huxford T."xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/author | "Phelps C.B."xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/author | "Mishler D."xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/author | "Sengchanthalangsy L.L."xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/name | "J Mol Biol"xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/pages | "587-597"xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/title | "Solvent exposed non-contacting amino acids play a critical role in NF-kappaB/IkappaBalpha complex formation."xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://purl.uniprot.org/core/volume | "324"xsd:string |
| http://purl.uniprot.org/citations/12460563 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12460563 |
| http://purl.uniprot.org/citations/12460563 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12460563 |
| http://purl.uniprot.org/uniprot/#_Q04207-mappedCitation-12460563 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/12460563 |
| http://purl.uniprot.org/uniprot/Q04207 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/12460563 |