(Figure Presented) New binding sites: Calcium(II) binding to the dimeric protein S100A13 triggers key conformational changes, thus creating two symmetrical copper(II)-binding sites between the helices of the monomers (see picture). These solvent-exposed binding sites are unique among the S100 proteins. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.
Structural interplay between calcium(II) and copper(II) binding to S100A13 protein / F.Arnesano; L.Banci; I.Bertini; A.Fantoni; L.Tenori; M.S.Viezzoli. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 44:(2005), pp. 6341-6344. [10.1002/anie.200500540]
Structural interplay between calcium(II) and copper(II) binding to S100A13 protein
BANCI, LUCIA;BERTINI, IVANO;TENORI, LEONARDO;VIEZZOLI, MARIA SILVIA
2005
Abstract
(Figure Presented) New binding sites: Calcium(II) binding to the dimeric protein S100A13 triggers key conformational changes, thus creating two symmetrical copper(II)-binding sites between the helices of the monomers (see picture). These solvent-exposed binding sites are unique among the S100 proteins. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.
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