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Review
. 2009 Mar;133(3):231-7.
doi: 10.1085/jgp.200810137.

Divide and conquer: high resolution structural information on TRP channel fragments

Rachelle Gaudet  1
Affiliations
Review

Divide and conquer: high resolution structural information on TRP channel fragments

Rachelle Gaudet. J Gen Physiol. 2009 Mar.
No abstract available

PubMed Disclaimer

Figures

Figure 1.
Figure 1.
The ankyrin repeats of TRPV channels. Diagram shows the topology of TRPV channels with the relative position of the ankyrin repeats illustrated with the structure of the TRPV1 ARD. Only two of the four subunits are shown for clarity in yellow and green, respectively; the subunits in front and in back of the plane of the page are omitted. The transmembrane domains are illustrated using the homologous structure of the Shaker potassium channel (Long et al., 2005). The N- and C-terminal segments of unknown structure are depicted with shapes that approximate their relative size. ATP and ATP-interacting side chains are shown as sticks and colored according to atom type, and a transparent surface representation highlights the surface complementarity of the ATP and its binding site. The approximate size of those protein segments in numbers of amino acid (aa) residues is indicated for the green subunit. The transmembrane and ARDs of TRPV channels are each ∼250 amino acid residues. TRPV subunits typically are ∼800-residues long.
Figure 2.
Figure 2.
The coiled-coils of TRPM channels. (A) Helical wheel representation of parallel (left) and antiparallel (right) tetrameric coiled-coils. The “N” or “C” in each wheel indicates whether the N or C terminus, respectively, of the α-helix points toward the viewer. Darker lines are in front and lighter ones are in the back. In both coiled-coils, the a and d residues of the heptad repeats form the core, whereas the e and g residues form peripheral interactions. However, the details of the interactions are different. In a parallel coiled-coil, each layer of hydrophobic interactions consists of either four a or four d residues. In contrast, each antiparallel layer consists of two d and two a residues. (B) Sequence alignment of the predicted coiled-coil sequences of human TRPM channels. The sequence of the rat TRPM7 coiled-coil, for which the structure is available, is also included at the top. a and d position residues are shaded. The dendrogram was generated by ClustalW using an alignment of whole TRPM sequences. (C) Diagram of TRPM7 displaying the available structural information. Similarly to Fig. 1, only two of the four channel subunits are illustrated for clarity (green and blue, respectively), except for the coiled-coil structure where all four strands are shown. Note that the transmembrane domain would have fourfold rotational symmetry perpendicular to the membrane (gray shading), whereas the coiled-coil and α-kinase domains only have twofold symmetry. Shape sizes approximate the number of residues in each region, and the size (in number of amino acid residues [aa]) is indicated for the blue subunit. The approximate boundaries, in residue numbers, of different domains are also indicated.
See this image and copyright information in PMC

References

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