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Calmodulin controls the rod photoreceptor CNG channel through an unconventional binding site in the N ‐ terminus of the β ‐ subunit by Dietmar Weitz, Martin.

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Presentation on theme: "Calmodulin controls the rod photoreceptor CNG channel through an unconventional binding site in the N ‐ terminus of the β ‐ subunit by Dietmar Weitz, Martin."— Presentation transcript:

1 Calmodulin controls the rod photoreceptor CNG channel through an unconventional binding site in the N ‐ terminus of the β ‐ subunit by Dietmar Weitz, Martin Zoche, Frank Müller, Michael Beyermann, Heinz G. Körschen, U. Benjamin Kaupp, and Karl ‐ Wilhelm Koch EMBO J. Volume 17(8):2273-2284 April 15, 1998 ©1998 by European Molecular Biology Organization

2 Location of putative CaM ‐ binding sites within the β ‐ subunit of the bovine rod CNG channel. Dietmar Weitz et al. EMBO J. 1998;17:2273-2284 ©1998 by European Molecular Biology Organization

3 Calmodulin binds to N ‐ and C ‐ terminal regions. Dietmar Weitz et al. EMBO J. 1998;17:2273-2284 ©1998 by European Molecular Biology Organization

4 Quantitative analysis of CaM binding to C ‐ terminal targets. Dietmar Weitz et al. EMBO J. 1998;17:2273-2284 ©1998 by European Molecular Biology Organization

5 Quantitative analysis of CaM binding to N ‐ terminal targets. Dietmar Weitz et al. EMBO J. 1998;17:2273-2284 ©1998 by European Molecular Biology Organization

6 Analysis of CaM ‐ binding with a reversed geometry. Dietmar Weitz et al. EMBO J. 1998;17:2273-2284 ©1998 by European Molecular Biology Organization

7 Semi ‐ quantitative analysis of CaM binding to peptides and fusion proteins in solution. Dietmar Weitz et al. EMBO J. 1998;17:2273-2284 ©1998 by European Molecular Biology Organization

8 Ca2+ dependence of CaM binding. Dietmar Weitz et al. EMBO J. 1998;17:2273-2284 ©1998 by European Molecular Biology Organization

9 Calmodulin and recoverin sensitivity of heterologously expressed CNG channels. Dietmar Weitz et al. EMBO J. 1998;17:2273-2284 ©1998 by European Molecular Biology Organization

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