| http://purl.uniprot.org/citations/15233806 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15233806 | http://www.w3.org/2000/01/rdf-schema#comment | "Microfibrils and elastin are major constituents of elastic fibers, the assembly of which is dictated by multimolecular interactions. Microfibril-associated glycoprotein-1 (MAGP-1) is a microfibrillar component that interacts with the soluble elastin precursor, tropoelastin. We describe here the adaptation of a solid-phase binding assay that defines the effect of divalent cations on the interactions between MAGP-1 and tropoelastin. Using this assay, a strong calcium-dependent interaction was demonstrated, with a dissociation constant of 2.8 +/-0.3 nm, which fits a single-site binding model. Manganese and magnesium bestowed a weaker association, and copper did not facilitate the protein interactions. Three constructs spanning tropoelastin were used to quantify their relative contributions to calcium-dependent MAGP-1 binding. Binding to a construct spanning a region from the N-terminus to domain 18 followed a single-site binding model with a dissociation constant of 12.0 +/-2.2 nm, which contrasted with the complex binding behavior observed for fragments spanning domains 17-27 and domain 27 to the C-terminus. To further elucidate binding sites around the kallikrein cleavage site of domains 25/26, MAGP-1 was presented with constructs containing C-terminal deletions within the region. Construct M1659, which spans a region from the N-terminus of tropoelastin to domain 26, inclusive, bound MAGP-1 with a dissociation constant of 9.7 +/- 2.0 nm, which decreased to 4.9 +/-1.0 nm following the removal of domain 26 (M155n), thus displaying only half the total capacity to bind MAGP-1. These results demonstrate that MAGP-1 is capable of cumulative binding to distinct regions on tropoelastin, with different apparent dissociation constants and different amounts of bound protein."xsd:string |
| http://purl.uniprot.org/citations/15233806 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.2004.04246.x"xsd:string |
| http://purl.uniprot.org/citations/15233806 | http://purl.uniprot.org/core/author | "Clarke A.W."xsd:string |
| http://purl.uniprot.org/citations/15233806 | http://purl.uniprot.org/core/author | "Weiss A.S."xsd:string |
| http://purl.uniprot.org/citations/15233806 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15233806 | http://purl.uniprot.org/core/name | "Eur J Biochem"xsd:string |
| http://purl.uniprot.org/citations/15233806 | http://purl.uniprot.org/core/pages | "3085-3090"xsd:string |
| http://purl.uniprot.org/citations/15233806 | http://purl.uniprot.org/core/title | "Microfibril-associated glycoprotein-1 binding to tropoelastin: multiple binding sites and the role of divalent cations."xsd:string |
| http://purl.uniprot.org/citations/15233806 | http://purl.uniprot.org/core/volume | "271"xsd:string |
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| http://purl.uniprot.org/uniprot/#_Q59H17-mappedCitation-15233806 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15233806 |