Add time:08/23/2019         Source:sciencedirect.com

Publisher SummaryThis chapter discusses the role of accessory proteins in G protein-coupled receptor signaling. The diversity of additional proteins that bind to GPCRs is bewildering; in many cases, the significance of the reaction is difficult to assess because a given receptor, clearly, cannot interact with these proteins simultaneously. The structure of G protein heterotrimers and of rhodopsin is known to atomic resolution. Hence, the sizes of the two proteins can be compared. The intracellular surface of rhodopsin barely suffices to cover the necessary contact sites on transducin. There is little, if any, space left to accommodate additional (bulky) proteins. The formation of receptor multimers may offer a way out; it suffices if one or a few receptors in a cluster are actually tethered to and immobilized by the scaffolding protein(s). Given their propensity to form complexes, the remaining receptors may aggregate by homo- and heterotypic aggregation. It is, in this context, interesting to note that G proteins can also form large aggregates in their basal state.

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