| http://purl.uniprot.org/citations/21848512 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21848512 | http://www.w3.org/2000/01/rdf-schema#comment | "In erythrocytes, 4.1R80 (80 kDa isoform of protein 4.1R) binds to the cytoplasmic tail of the transmembrane proteins band 3 and GPC (glycophorin C), and to the membrane-associated protein p55 through the N- (N-terminal), α-(α-helix-rich) and C-(C-terminal) lobes of R30 [N-terminal 30 kDa FERM (4.1/ezrin/radixin/moesin) domain of protein 4.1R] respectively. We have shown previously that R30 binds to CaM (calmodulin) in a Ca2+-independent manner, the equilibrium dissociation constant (Kd) for R30-CaM binding being very similar (in the submicromolar range) in the presence or absence of Ca2+. In the present study, we investigated the consequences of CaM binding on R30's structural stability using resonant mirror detection and FTIR (Fourier-transform IR) spectroscopy. After a 30 min incubation above 40° C, R30 could no longer bind to band 3 or to GPC. In contrast, R30 binding to p55, which could be detected at a temperature as low as 34° C, was maintained up to 44° C in the presence of apo-CaM. Dynamic light scattering measurements indicated that R30, either alone or complexed with apo-CaM, did not aggregate up to 40° C. FTIR spectroscopy revealed that the dramatic variations in the structure of the β-sheet structure of R30 observed at various temperatures were minimized in the presence of apo-CaM. On the basis of Kd values calculated at various temperatures, ΔCp and ΔG° for R30 binding to apo-CaM were determined as -10 kJ · K(-1) · mol-1 and ~ -38 kJ · mol(-1) at 37° C (310.15 K) respectively. These data support the notion that apo-CaM stabilizes R30 through interaction with its β-strand-rich C-lobe and provide a novel function for CaM, i.e. structural stabilization of 4.1R80."xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20110676"xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://purl.uniprot.org/core/author | "Nakamura S."xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://purl.uniprot.org/core/author | "Kidokoro S."xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://purl.uniprot.org/core/author | "Shiba K."xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://purl.uniprot.org/core/author | "Takakuwa Y."xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://purl.uniprot.org/core/author | "Nunomura W."xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://purl.uniprot.org/core/author | "Sasakura D."xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21848512 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://purl.uniprot.org/core/pages | "367-374"xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://purl.uniprot.org/core/title | "Structural stabilization of protein 4.1R FERM domain upon binding to apo-calmodulin: novel insights into the biological significance of the calcium-independent binding of calmodulin to protein 4.1R."xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://purl.uniprot.org/core/volume | "440"xsd:string |
| http://purl.uniprot.org/citations/21848512 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21848512 |
| http://purl.uniprot.org/citations/21848512 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21848512 |
| http://purl.uniprot.org/uniprot/#_A0A2R8Y7Y3-mappedCitation-21848512 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21848512 |
| http://purl.uniprot.org/uniprot/#_A0A2R8YD30-mappedCitation-21848512 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21848512 |
| http://purl.uniprot.org/uniprot/#_P11171-mappedCitation-21848512 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21848512 |
| http://purl.uniprot.org/uniprot/#_B7Z5L2-mappedCitation-21848512 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21848512 |
| http://purl.uniprot.org/uniprot/#_B7Z627-mappedCitation-21848512 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21848512 |
| http://purl.uniprot.org/uniprot/#_Q4VB86-mappedCitation-21848512 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21848512 |
| http://purl.uniprot.org/uniprot/#_Q4VB87-mappedCitation-21848512 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21848512 |
| http://purl.uniprot.org/uniprot/#_Q59F12-mappedCitation-21848512 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21848512 |
| http://purl.uniprot.org/uniprot/#_Q29RX4-mappedCitation-21848512 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21848512 |