| Unique identifier for interactor A | uniprotkb:P01130 |
| Unique identifier for interactor B | uniprotkb:P01130 |
| Alternative identifier for interactor A | intact:EBI-988319 uniprotkb:B4DJZ8 uniprotkb:C0JYY8 uniprotkb:Q9UDH7 uniprotkb:B4DR00 uniprotkb:B4DTQ3 uniprotkb:H0YLU8 uniprotkb:Q59FQ1 uniprotkb:B4DII3 uniprotkb:H0YNT7 ensembl:ENSP00000454071.1 uniprotkb:Q53ZD9 |
| Alternative identifier for interactor B | intact:EBI-988319 uniprotkb:B4DJZ8 uniprotkb:C0JYY8 uniprotkb:Q9UDH7 uniprotkb:B4DR00 uniprotkb:B4DTQ3 uniprotkb:H0YLU8 uniprotkb:Q59FQ1 uniprotkb:B4DII3 uniprotkb:H0YNT7 ensembl:ENSP00000454071.1 uniprotkb:Q53ZD9 |
| Aliases for A | psi-mi:ldlr_human(display_long) uniprotkb:LDLR(gene name) psi-mi:LDLR(display_short) |
| Aliases for B | psi-mi:ldlr_human(display_long) uniprotkb:LDLR(gene name) psi-mi:LDLR(display_short) |
| Interaction detection methods | psi-mi:"MI:0107"(surface plasmon resonance) |
| First author | Martínez-Oliván et al. (2015) |
| Identifier of the publication | pubmed:26526611 imex:IM-24943 |
| NCBI Taxonomy identifier for interactor A | taxid:9606(human) taxid:9606(Homo sapiens) |
| NCBI Taxonomy identifier for interactor B | taxid:9606(human) taxid:9606(Homo sapiens) |
| Interaction types | psi-mi:"MI:0407"(direct interaction) |
| Source databases and identifiers | psi-mi:"MI:0471"(MINT) |
| Interaction identifier(s) in the corresponding source database | intact:EBI-11476421 imex:IM-24943-3 |
| Confidence score | intact-miscore:0.44 |
| Complex expansion | - |
| Biological role A | Unspecified role |
| Biological role B | Unspecified role |
| Experimental role A | Bait |
| Experimental role B | Prey |
| Interactor type A | Protein |
| Interactor type B | Protein |
| Annotations for the interaction | figure legend:f2 t1 f3 comment:"\"Our SPR experiments reveal that, in absence of calcium, binding of LR4–5 to the BβC fragment is markedly reduced (Fig. 2 and Fig. 3, Table 1). At pH 5.5, with 0.25 mM EDTA, 60 μM of LR4–5 saturate 17.1% of the immobilized ligands after 60 s, 4 times less than the binding observed in presence of 1.5 mM CaCl2 under the same conditions (Fig. 2 and Fig. 3, Table 1). Similarly, under the same conditions, LR5 binding is slightly reduced without calcium, from 3.0% to 2.1% of Rmax (Fig. 2, Table 1), and LR4 binding is drastically reduced from 22.5% with calcium to 3.5% without the cation (Fig. 2, Table 1). Not surprisingly, depletion of calcium causes a greater effect on the binding of LR4 than on that of LR5, consistent with the larger conformational change reported for LR4 when it unfolds and releases Ca++ at pH 5.5 [41]. As it appears, both high calcium concentrations and low pH promote binding of LR domains to the β-propeller. At pH 7.0, with 0.25 mM EDTA, only residual binding to the β-propeller is observed for the LR4–5 pair, reaching 0.7% of Rmax after 60 s injection of LR4–5 (Fig. 2 and Fig. 3, Table 1), and we could not detect binding of the β-propeller to the isolated LR4 or LR5 modules (Fig. 2, Table 1).\"" full coverage:Only protein-protein interactions curation depth:imex curation |
| NCBI Taxonomy identifier for the host organism | taxid:-1(in vitro) taxid:-1(In vitro) |
| Parameters of the interaction | kd:3.5x10^-6(molar) |
| Creation date | 2016/01/11 |
| Update date | 2016/01/11 |
| negative Boolean value | false |
| Feature(s) for interactor A | binding-associated region:400-657 |
| Feature(s) for interactor B | binding-associated region:142-186 |
| Stoichiometry for interactor A | - |
| Stoichiometry for interactor B | - |
| Participant identification method for interactor A | Predetermined participant |
| Participant identification method for interactor B | Predetermined participant |