Transient Receptor Potential Channels
Transient Receptor Potential Channels offers a unique blend of thoughtfully selected topics ranging from the structural biology of this fascinating group of ion channels to their emerging roles in human diseases. This single book covers TRP channels of ye
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Structural Biology of TRP Channels Minghui Li, Yong Yu, and Jian Yang
Abstract Structural studies on TRP channels, while limited, are poised for a quickened pace and rapid expansion. As of yet, no high-resolution structure of a full length TRP channel exists, but low-resolution electron cryomicroscopy structures have been obtained for 4 TRP channels, and high-resolution NMR and X-ray crystal structures have been obtained for the cytoplasmic domains, including an atypical protein kinase domain, ankyrin repeats, coiled coil domains and a Ca2+ binding domain, of 6 TRP channels. These structures enhance our understanding of TRP channel assembly and regulation. Continued technical advances in structural approaches promise a bright outlook for TRP channel structural biology.
1.1 Introduction Full understanding of ion channel function requires high-resolution threedimensional (3D) structures. Structural studies on ion channels entered a new phase in 1998 after the publication of the crystal structure of the bacterial K+ channel, KcsA [1]. Since then, there has been a rapid growth in the number of ion channel structures. To date, there are ~90 crystal structures of full length or near full length ion channels, ~50 electron microscopy structures of full length or near full length ion channels, and ~130 crystal and nuclear magnetic resonance (NMR) structures of ion channel fragments. These structures have led to a quantum leap in our understanding of the molecular and biophysical mechanisms of ion channel assembly, selectivity, conduction, gating and regulation. TRP channels constitute a distinct superfamily of ion channels and are distantly related to voltage-gated K+ , Na+ and Ca2+ superfamilies. They are expressed and function in diverse organisms, including yeasts, worms, fruit flies, mice and humans. Excluding yeast TRPs, there are seven subfamilies: TRPC, TRPV, TRPM, TRPA,
J. Yang (B) Department of Biological Sciences, Columbia University, New York, NY 10027, USA e-mail: [email protected] M.S. Islam (ed.), Transient Receptor Potential Channels, Advances in Experimental Medicine and Biology 704, DOI 10.1007/978-94-007-0265-3_1, C Springer Science+Business Media B.V. 2011
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Fig. 1.1 TRP channel subfamilies and the transmembrane topology and domain organization of their subunits. Only commonly present and readily identifiable domains or motifs in the cytoplasmic N and C termini are indicated. Examples of high-resolution structures of some domains or motifs are presented
TRPN, TRPP and TRPML, with TRPN absent in mice and humans (Fig. 1.1) [2]. Each subfamily has one or more members. Mice have a total of 28 different members, and humans 27. All TRP channel subunits have six putative transmembrane segments and a pore-forming loop between the last two transmembrane segments (Fig. 1.1). The amino (N) and carboxyl (C) termini are located intracellularly and vary vastly in length (Table 1.1) and amino acid (aa) sequence. These cytoplasmic regions contain various well-recognized domains and motifs that
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