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  • Title: Insights into functional aspects of centrins from the structure of N-terminally extended mouse centrin 1.
    Author: Park JH, Pulvermüller A, Scheerer P, Rausch S, Giessl A, Höhne W, Wolfrum U, Hofmann KP, Ernst OP, Choe HW, Krauss N.
    Journal: Vision Res; 2006 Dec; 46(27):4568-74. PubMed ID: 17027898.
    Abstract:
    Centrins are members of the family of Ca(2+)-binding EF-hand proteins. In photoreceptor cells, centrin isoform 1 is specifically localized in the non-motile cilium. This connecting cilium links the light-sensitive outer segment with the biosynthetic active inner segment of the photoreceptor cell. All intracellular exchanges between these compartments have to occur through this cilium. Three-dimensional structures of centrins from diverse organisms are known, showing that the EF-hand motifs of the N-terminal domains adopt closed conformations, while the C-terminal EF-hand motifs have open conformations. The crystal structure of an N-terminally extended mouse centrin 1 (MmCen1-L) resembles the overall structure of troponin C in its two Ca(2+) bound form. Within the N-terminal extension in MmCen1-L, residues W24 and R25 bind to the C-terminal domain of centrin 1 in a target-protein-like geometry. Here, we discuss this binding mode in connection with putative interaction sites of the target-protein transducin and the self-assembly of centrins.
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