Ryanodine receptors: Structure and macromolecular interactions

Current Opinion in Structural Biology

Volumn 7, Issue 2, 1997, Pages 258-264

  Wagenknecht, Terence ^a   Radermacher, Michael ^a  

^a WADSWORTH CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; RYANODINE RECEPTOR;

CALCIUM CELL LEVEL; CRYOELECTRON MICROSCOPY; IMAGE RECONSTRUCTION; MACROMOLECULE; PRIORITY JOURNAL; RECEPTOR BINDING; REVIEW; SARCOPLASMIC RETICULUM; STRUCTURE ACTIVITY RELATION;

EID: 0030904525     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80034-6     Document Type: Article

References (55)

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26. •] also compare the results with a previous 3D reconstruction of negatively stained RyR, which demonstrates the severe distortions of the receptor that occur upon air drying in the presence of stain.
27. •) in which conditions favoring the closed state are employed. Remarkably, even at the modest resolution achievable (3nm), a comparison of the two reconstructions shows differences in both the transmembrane and cytoplasmic regions of the receptor (see 'Evidence for global conformation changes'). A proviso of these studies is the assumption that the activating and inactivating conditions established for physiological conditions also apply to the nonphysiological conditions (detergent-solubilized receptors) actually used.
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44. •] of the structure and macromolecular interactions of triadin is presented. Evidence is reported that shows that triadin binds to both the DHPR and RyR, and hence might be responsible for linking the RyR and DHPR at the triad junction. No interaction between the DHPR and RyR is detectable. An alternative model for the transmembrane topology of triadin is also discussed in the accompanying paper [63].
45. •].
46. •] find that the II-III loop might actually consist of two domains, one of which activates the RyR, and the other which antagonizes the activation, and they hypothesize that the voltage-sensing property of the DHPR could involve a change in the relative contributions of these two domains' activities.
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