info:eu-repo/semantics/article
Engineered chimeras reveal the structural basis of hexacoordination in globins: A case study of neuroglobin and myoglobin
Fecha
2014-10Registro en:
Boron, Carlos Ignacio; Capece, Luciana; Pennacchietti, Francesca; Wetzler, Diana Elena; Bruno, Stefano; et al.; Engineered chimeras reveal the structural basis of hexacoordination in globins: A case study of neuroglobin and myoglobin; Elsevier Science; Biochimica et Biophysica Acta - General Subjects; 1850; 1; 10-2014; 169-177
0304-4165
CONICET Digital
CONICET
Autor
Boron, Carlos Ignacio
Capece, Luciana
Pennacchietti, Francesca
Wetzler, Diana Elena
Bruno, Stefano
Abbruzzetti, Stefania
Chisari, Lucía
Luque, F. Javier
Viappiani, Cristiano
Marti, Marcelo Adrian
Estrin, Dario Ariel
Nadra, Alejandro Daniel
Resumen
Background Myoglobin (Mb) and neuroglobin (Ngb) are representative members of pentacoordinated and bis-histidyl, hexacoordinated globins. In spite of their low sequence identity, they show surprisingly similar three-dimensional folds. The ability of Ngb to form a hexacoordinated bis-histidyl complex with the distal HisE7 has a strong impact on ligand affinity. The factors governing such different behaviors have not been completely understood yet, even though they are extremely relevant to establish structure-function relationships within the globin superfamily.