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Titolo:
The functional similarity and structural diversity of human and cartilaginous fish hemoglobins
Autore:
Naoi, Y; Chong, KT; Yoshimatsu, K; Miyazaki, G; Tame, JRH; Park, SY; Adachi, S; Morimoto, H;
Indirizzi:
Osaka Univ, Grad Sch Engn Sci, Div Biophys Engn, Toyonaka, Osaka 5608531, Japan Osaka Univ Toyonaka Osaka Japan 5608531 n, Toyonaka, Osaka 5608531, Japan Osaka Univ, Inst Prot Res, Toyonaka, Osaka 5600871, Japan Osaka Univ Toyonaka Osaka Japan 5600871 s, Toyonaka, Osaka 5600871, Japan JST, ERATO, Proton Nanomachine Project, Kyoto 6190237, Japan JST Kyoto Japan 6190237 Proton Nanomachine Project, Kyoto 6190237, Japan RIKEN, Harima Inst, Inst Phys & Chem Res, Sayo, Hyogo 6795143, Japan RIKEN Sayo Hyogo Japan 6795143 hys & Chem Res, Sayo, Hyogo 6795143, Japan
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 1, volume: 307, anno: 2001,
pagine: 259 - 270
SICI:
0022-2836(20010316)307:1<259:TFSASD>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
X-RAY-DIFFRACTION; CRYSTAL-STRUCTURE; PAGOTHENIA-BERNACCHII; OXYGEN-AFFINITY; LIGAND-BINDING; RESOLUTION; DEOXY; DEOXYHEMOGLOBIN; REFINEMENT; SUPEROXIDE;
Keywords:
vertebrate hemoglobin; X-ray crystallography; molecular evolution; shark; structural comparison;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Naoi, Y Kyoto Univ, Food Sci Res Inst, Gokasho, Uji, Kyoto 6110011, Japan Kyoto Univ Gokasho Uji Kyoto Japan 6110011 i, Kyoto 6110011, Japan
Citazione:
Y. Naoi et al., "The functional similarity and structural diversity of human and cartilaginous fish hemoglobins", J MOL BIOL, 307(1), 2001, pp. 259-270

Abstract

Although many descriptions of adaptive molecular evolution of vertebrate hemoglobins (Hb) can be found in physiological text books, they are based mainly on changes of the primary structure and place more emphasis on conservation than alterations at the functional site. Sequence analysis alone, however, does not reveal much about the evolution of new functions in proteinsIt was found recently that there are many functionally important structural differences between human and a ray (Dasyatis akajei) I FD even where sequence is conserved between the two. We have solved the structures of the deoxy and CO forms of a second cartilaginous fish (a shark, Mustelus griseus)Hb, and compared it with structures of human Hb, two bony fish Hbs and theray Hb in order to understand more about how vertebrate Hbs have functionally evolved by the selection of random amino acid substitutions. The sequence identity of cartilaginous fish Hb and human Hb is a little less than 40 %, with many functionally important amino acid replacements. Wider substitutions than usually considered as neutral have been accepted in the course of molecular evolution of Hb. As with the ray Hb, the shark Hb shows functionally important structural differences from human Hb that involve amino acid substitutions and shifts of preserved amino acid residues induced by substitutions in other parts of the molecule. Most importantly, beta E11Val in deoxy human Hb, which overlaps the ligand binding site and is considered toplay a key role in controlling the oxygen affinity, moves away about 1 A in both the shark and ray Hbs. Thus adaptive molecular evolution is feasibleas a result of both functionally significant mutations and deviations of preserved amino acid residues induced by other amino acid substitutions. (C)2001 Academic Press.

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Documento generato il 27/11/20 alle ore 13:43:41