期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 70, 期 -, 页码 1640-1648出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1399004714007032
关键词
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资金
- Ministero dell' Istruzione, dell'Universita e della Ricerca of Italy [2007B57EAB_004, 20074TJ3ZB_005, RBRN07BMCT_007]
- Ministero dell' Istruzione, dell'Universita e della Ricerca of Italy (PNR-CNR Aging Program)
- European Community under BioStruct-X [283570]
- European Community-Research Infrastructure Action from the FP6 'Structuring the European Research Area Programme' [RII3-CT-2004-506008]
Neuroglobin is a member of the globin family involved in neuroprotection; it is primarily expressed in the brain and retina of vertebrates. Neuroglobin belongs to the heterogeneous group of hexacoordinate globins that have evolved in animals, plants and bacteria, endowed with the capability of reversible intramolecular coordination, allowing the binding of small gaseous ligands (O-2, NO and CO). In a unique fashion among haemoproteins, ligand-binding events in neuroglobin are dependent on the sliding of the haem itself within a preformed internal cavity, as revealed by the crystal structure of its CO-bound derivative. Point mutants of the neuroglobin internal cavity have been engineered and their functional and structural characterization shows that hindering the haem displacement leads to a decrease in CO affinity, whereas reducing the cavity volume without interfering with haem sliding has negligible functional effects.
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