The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the α-helical globin fold

Structure

Volumn 10, Issue 5, 2002, Pages 725-735

  Pesce, Alessandra ^a   Nardini, Marco ^a   Dewilde, Sylvia ^b   Geuens, Eva ^b   Yamauchi, Kiyoshi ^c   Ascenzi, Paolo ^a,d   Riggs, Austen F ^e   Moens, Luc ^b   Bolognesi, Martino ^a  

^a UNIVERSITY OF GENOA   (Italy)

^b UNIVERSITY OF ANTWERP   (Belgium)

^c SHIZUOKA UNIVERSITY   (Japan)

^d ROMA TRE UNIVERSITY   (Italy)

^e UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

Globin fold plasticity; Nerve tissue minihemoglobin; Oxygen binding; Oxygenated hemoglobin; Protein cavities; X ray crystallography

Indexed keywords

AROMATIC COMPOUND; GLOBIN; GLUTAMINE; HEME; HEMOGLOBIN; OXYGEN; SOLVENT; TYROSINE; NERVE PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANOXIA; ARTICLE; CELL ACTIVITY; CONTROLLED STUDY; CRYSTAL STRUCTURE; GENE DELETION; HYDROGEN BOND; NERVE CELL; NERVOUS TISSUE; NONHUMAN; PLASTICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; PROTEIN VARIANT; SEQUENCE ANALYSIS; WORM; X RAY CRYSTALLOGRAPHY; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; INVERTEBRATE; METABOLISM; MOLECULAR GENETICS; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITES; HEMOGLOBINS; HUMAN; INVERTEBRATES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; NERVE TISSUE PROTEINS; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SUPPORT, NON-U.S. GOV'T; ANIMALS; HUMANS;

CEREBRATULUS; CEREBRATULUS LACTEUS; NEMERTEA;

EID: 0036098845     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00763-3     Document Type: Article

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