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Figure 1 | BMC Bioinformatics

Figure 1

From: Structural fragment clustering reveals novel structural and functional motifs in α-helical transmembrane proteins

Figure 1

A- [AS]- [FIV]- [NR]-A-P-L- [AT]-G motif. Voltage-gated chloride channel, dimeric form (PDB ID: 1kpl, chain: B). The two reentrant regions where the A- [AS]- [FIV]- [NR]-A-P-L- [AT]-G motif is found are shown in red. The sequences of the two reentrant regions are also shown. A multiple sequence alignment of several bacterial chloride channels (derived from a PSI-BLAST search against Swiss-Prot with the 1kpl sequence, data not shown) shows that A- [AS]- [FIV]- [NR]-A-P-L- [AT]-G motif is well conserved across different bacteria (see Logo in the picture), indicating its possible functional implication. At the bottom: a zoomed-in view of a portion of the voltage-gated chloride channel dimerization interface. The residues belonging to the reentrant regions and part of the A- [AS]- [FIV]- [NR]-A-P-L- [AT]-G motif are highlighted in red. The interface residues that are less that 5 Å apart from the red residues are shown in gray.

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BMC Bioinformatics

ISSN: 1471-2105

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