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Structural Research of Mechanosensitive Channels

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Mechanosensitive channels (MSC) are membrane proteins capable of responding to mechanical stress in response to external mechanical stimuli. In living organisms, MSC is used to sense mechanical stimuli and convert physical stresses on cell membranes into electrochemical reactions that enable them to respond accordingly.

Research Progress on the Structure of MSC in Prokaryotes

In prokaryotes, the small conductance mechanosensitive channels MScS are homoheptamers, each subunit containing three transmembrane domains, with the n end facing the membrane and the c end embedded in the cytoplasm. Large conductivity force-sensitive channel (MScL) is a homopentameter. It is mainly composed of helical regions opposite the bilayer. Contains two domains. In the MScL structure, the helix passes through the membrane twice at the C and N ends.

Research Progress on the Structure of MSC in Eukaryotes

Among eukaryotes, the TRP protein is the best-known MSC. The TRP protein has a pore between the transmembrane domains S5 and S6. They contain intracellular N and C ends, forming a tetramer. TRP proteins mediate protein interactions and help stretch activation channels open.

X-ray crystallography and low-temperature electron microscopy have been used to study the structure of MSC Proteins. The structural information obtained from experiments can help scientists gain insight into the response to mechanical stress mechanisms in living organisms.

Architecture and domain organization of crTRP1Figure 1. Architecture and domain organization of crTRP1. (McGoldrick L L, et al., 2019)

Protein Organism Method Resolution PDB Entry ID
Thermo-Sensitive TRP Channel TRP1 from the Alga Chlamydomonas reinhardtii Chlamydomonas reinhardtii Cryo-EM single particle analysis 3.45 Å 6PW5
TRPC3 in a lipid-occupied, closed state Homo sapiens Cryo-EM single particle analysis 3.30 Å 6CUD
Canonical TRPC4 ion channel Danio rerio Cryo-EM single particle analysis 3.60 Å 6G1K
Human TRPC6 Homo sapiens Cryo-EM single particle analysis 3.80 Å 5YX9
Coiled-coil domain of the transient receptor potential channel from Gibberella zeae (TRPGz) Fusarium graminearum PH-1 X-ray diffraction 1.25 Å 3VVI
TRPV6 ankyrin repeat domain Mus musculus X-ray diffraction 1.70 Å 2RFA
Ankyrin repeat domain of human TRPV2 Homo sapiens X-ray diffraction 1.70 Å 2F37
Cold- and menthol-sensing ion channel TRPM8 Ficedula albicollis Cryo-EM single particle analysis 4.10 Å 6BPQ
TRPML3 ion channel Callithrix jacchus Cryo-EM single particle analysis 2.94 Å 5W3S
Small-molecule modulation of acid-sensing ion channel 1 (ASIC1) Gallus gallus X-ray diffraction 3.01 Å 6X9H
Zebrafish two pore domain K+ channel TREK1 (K2P2.1) in DDM/POPA mixed micelles Danio rerio Cryo-EM single particle analysis 2.82 Å 8DE8
Human two pore domain potassium ion channel TREK2 (K2P10.1) Homo sapiens X-ray diffraction 3.20 Å 4BW5
Human ASIC1a-Nb.C1 complex Homo sapiens Cryo-EM single particle analysis 2.86 Å 7RNN

Table 1. Structural research of mechanosensitive channels.

Structural analysis of mechanosensitive channels using cryo-electron microscopy (cryo-EM) and X-ray crystallography are beneficial for further research of their functions. Creative Biostructure has expertise and experience in membrane protein research. We offer cryo-EM services to determine the structure of membrane proteins using single particle analysis (SPA).

In addition to the structural determination of membrane proteins, we can also accurately analyze nucleic acids, small proteins, ribosomes, protein complexes, protein-ligand complexes, and viruses. If you are interested in our services, please contact us.

References

  1. Geoffrey Chang, et al. Structure of the MscL Homolog from Mycobacterium tuberculosis: A Gated Mechanosensitive Ion Channel. Science, 1998, 282:2220-2226.
  2. Del Valle ME, et al. Mechanosensory neurons, cutaneous mechanoreceptors, and putative mechanoproteins. Microsc Res Tech. 2012 ,75(8):1033-1034.
  3. McGoldrick L L, et al. Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii. Nature Communications, 2019, 10(1): 4180.
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