| http://purl.uniprot.org/citations/18767159 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18767159 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18767159 | http://www.w3.org/2000/01/rdf-schema#comment | "Heat shock response (HSR) is a ubiquitous cellular mechanism that copes with a variety of stresses. This response is mediated by a family of transcriptional activators, heat shock factors (HSFs), which are under tight regulation. HSF binding protein 1 (HSBP1) is a negative regulator of HSR and is reported to bind specifically with the active trimeric form of HSF1, thus inhibiting its activity. HSBP1 contains heptad-repeats in the primary sequence and was believed to stay in a trimer form in solution. We report the crystal structure of the trimerization domain of the M30I/L55P mutant of human HSBP1 at 1.8 A resolution. In this crystal form, the HSBP1 fragment of residues 6-53 forms a continuous, 11-turn long helix. The helix self-associates to form a parallel, symmetrical, triple coiled-coil helix bundle, which further assembles into a dimer of trimers in a head-to-head fashion. Solution study confirmed that the wild-type HSBP1 shares similar biophysical properties with the crystallized variant. Furthermore, we identified Ser31, which buried its polar side chain in the hydrophobic interior of the helix bundle, as a stability weak-spot. Substitution of this residue with Ile increases the melting temperature by 24 degrees C, implicating that this conserved serine residue is maintained at position 31 for functional purposes."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.org/dc/terms/identifier | "doi:10.1002/prot.22216"xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.org/dc/terms/identifier | "doi:10.1002/prot.22216"xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Liu Y."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Liu Y."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Liu X."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Liu X."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Li X."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Li X."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Rao Z."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Rao Z."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Xu L."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Xu L."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Zhu G."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Zhu G."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Zhang X.C."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Zhang X.C."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Tong X."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/author | "Tong X."xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/name | "Proteins"xsd:string |
| http://purl.uniprot.org/citations/18767159 | http://purl.uniprot.org/core/name | "Proteins"xsd:string |