Figure 1 | Scientific Reports

Figure 1

From: Preferential selection of Arginine at the lipid-water-interface of TRPV1 during vertebrate evolution correlates with its snorkeling behaviour and cholesterol interaction

Figure 1

Preferential selection of snorkeling amino acids located at the lipid-water interface of TRPV1 during vertebrate evolution. (a,b) Schematic representation of hTRPV1 sequence in lipid bilayer made of POPC (left) and PEA (right) is shown. Residues located at the lipid-water interface are highlighted (red and green indicate the residues at the N-terminal and C-terminal of each TM helices respectively. Yellow indicates few residues that are common for both N-terminal and C-terminal of each TM helices, between TM3 & TM4 as well as TM4 & TM5). (c,d) Box plot showing conservation of 5 amino acid stretch sequences (marking the amino acids present in LWI) in each side of the TM made of POPC(left) and PEA(right) membrane. The LWI residues present in the inner leaflet of the membrane are highly conserved in vertebrates. (e,f) Conservation analysis of each residue present in the LWI. Snorkeling amino acids such as Arg and Tyr are highly conserved in the LWI of TRPV1. The residues which demarcate the exact boundary-point of individual TM in lipid bilayer are indicated by red colour asterisks (*).

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