Figure 6.
Figure 6. Disulfide-cross-linked Ca2+-CaM–TRPV1-CT35 complexes do not interact with TRPV1-ARD. (A) Ribbon diagram of TRPV1-CT35 (cyan) bound to Ca2+–CaM (gray) with modeled disulfide bonds (pink) based on predictions using SSBOND (Hazes and Dijkstra, 1988). (B) Native-PAGE of CaM or CaM cysteine mutants alone or in the presence of increasing molar ratio of respective TRPV1-CT or TRPV1-CT mutant. (C) Tricine–SDS-PAGE of CaM and TRPV1-CT35 cysteine mutants under reducing or oxidizing conditions. (D) 60 µM of purified rat TRPV1-ARD (RnARD) was mixed with 60 µM CaM (left), 60 µM of the cross-linked complex CaME127C–V1-CT35R785C (middle), or 60 µM CaMA15C–V1-CT35N789C (right) in the presence of CaCl2 and separated using SEC.

Disulfide-cross-linked Ca2+-CaM–TRPV1-CT35 complexes do not interact with TRPV1-ARD. (A) Ribbon diagram of TRPV1-CT35 (cyan) bound to Ca2+–CaM (gray) with modeled disulfide bonds (pink) based on predictions using SSBOND (Hazes and Dijkstra, 1988). (B) Native-PAGE of CaM or CaM cysteine mutants alone or in the presence of increasing molar ratio of respective TRPV1-CT or TRPV1-CT mutant. (C) Tricine–SDS-PAGE of CaM and TRPV1-CT35 cysteine mutants under reducing or oxidizing conditions. (D) 60 µM of purified rat TRPV1-ARD (RnARD) was mixed with 60 µM CaM (left), 60 µM of the cross-linked complex CaME127C–V1-CT35R785C (middle), or 60 µM CaMA15C–V1-CT35N789C (right) in the presence of CaCl2 and separated using SEC.

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