The role of histidine in a copper-specific metallothionein
Metallothioneins achieve metal binding specificity by modulation of their amino acid sequences through evolution. Non-coordinating residues seem to play a key role in this function, and among them histidine may be of particular importance. Here we report how this residue regulates CuI binding to a h...
| Autores: | , , , , , |
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| Tipo de documento: | artigo |
| Estado: | Versão publicada |
| Data de publicação: | 2013 |
| País: | Argentina |
| Recursos: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositório: | CONICET Digital (CONICET) |
| Idioma: | inglês |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/7830 |
| Acesso em linha: | http://hdl.handle.net/11336/7830 |
| Access Level: | Acceso aberto |
| Palavra-chave: | Metallothioneins Histidine Cu-Thionein Helix Pomatia https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| Resumo: | Metallothioneins achieve metal binding specificity by modulation of their amino acid sequences through evolution. Non-coordinating residues seem to play a key role in this function, and among them histidine may be of particular importance. Here we report how this residue regulates CuI binding to a highly copper specific isoform, the CuMT of the snail Helix pomatia, by analysis of the recombinant complexes yielded by a constructed mutant where this residue has been changed to an alanine. |
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