http://www.cnr.it/ontology/cnr/individuo/prodotto/ID1426

Protein fold and structure in the truncated (2/2) globin family (Articolo in rivista)

Type

Prodotto della ricerca (Classe)
Articolo in rivista (Classe)

Label

Protein fold and structure in the truncated (2/2) globin family (Articolo in rivista) (literal)

Anno

2007-01-01T00:00:00+01:00 (literal)

Alternative label

Nardini, M; Pesce, A; Milani, M; Bolognesi, M (2007)
Protein fold and structure in the truncated (2/2) globin family
in Gene (Amst.)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Nardini, M; Pesce, A; Milani, M; Bolognesi, M (literal)

Pagina inizio

2 (literal)

Pagina fine

11 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

398 (literal)

Rivista

Gene (Rivista)

Note

ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

Univ Milan, CNR, INFM, Dept Biomol Sci & Biotechnol, I-20131 Milan, Italy; Univ Genoa, CNR, INFM, Dept Phys, I-16146 Genoa, Italy; Univ Genoa, Ctr Excellence Biomed Res, I-16146 Genoa, Italy (literal)

Titolo

Protein fold and structure in the truncated (2/2) globin family (literal)

Abstract

Analysis of amino acids sequences and protein folds has recently unraveled the structural bases and details of several proteins from the recently discovered 'truncated hemoglobin' family. The analysis here presented, in agreement with previous surveys, shows that truncated hemoglobins can be classified in three main groups, based on their structural properties. Crystallographic analyses have shown that all three groups adopt a 2-on-2 alpha-helical sandwich fold, resulting from apparent editing of the classical 3-on-3 alpha-helical sandwich of vertebrate and invertebrate conventional globins. Specific structural features distinguish each of the three groups. Among these, a protein matrix tunnel system is typical of group 1, a Trp residue at the G8 topological site is conserved in groups 11 and 111, and TyrB10 is almost invariant through the three groups. A strongly intertwined network of hydrogen bonds stabilizes the heme bound ligand, despite variability of the heme distal residues observed in the different proteins considered. Details of ligand recognition in the three groups are discussed at the light of residue conservation and of differing ligand diffusion pathways to the heme. Based on structural analyses of the family-specific fold, we endorse a recent proposal of leaving the 'truncated hemoglobins' term, that does not represent properly the observed 2-on-2 alpha-helical sandwich fold, and adopting the simple '2/2Hb' term to concisely address this protein family. 0 2007 Elsevier B.V. All rights reserved. (literal)

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