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. 2011 Mar 14;208(3):577–592. doi: 10.1084/jem.20100619

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© 2011 Wang et al.

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Figure 1. — Sequence and structural analysis of VISTA. (A) The primary amino acid sequence of mouse VISTA with the Ig-V domain, the stalk segment, and the transmembrane region highlighted in blue, green, and red, respectively. Cysteines in the ectodomain region are indicated by underlining. (B) A comparative protein structure model of mouse VISTA using PD-L1 as the template (Protein Data Bank accession no. 3BIS). The five cysteine residues in the Ig-V domain are illustrated as orange sticks. Based on this model, the VISTA Ig-V domain has the canonical disulfide bond between the B and F strands, as well as three additional cysteines, some of which can potentially form inter- and intramolecular disulfide bonds. An additional invariant cysteine is present in the stalk region following the G strand (not depicted). The β strands (A–G) are marked as green and blue. The C″-D loop is marked by an arrow. (C) Multiple sequence alignment of the Ig-V domains of several B7 family members and VISTA. The predicted secondary structure (using arrows, springs, and “T”s for strands, helices, and β-turns, respectively) is marked above the alignment and is based on the VISTA structural model. (D) Multiple sequence alignment of VISTA orthologues. Invariant residues are represented by the red background, and physico-chemically conserved positions are represented by red letters. Conserved amino acids are marked by blue boxes. Conservation is calculated on the basis of 36 VISTA orthologous proteins, but only 9 representatives are shown. The canonical cysteine pair (B and F strands) that is conserved in almost all Ig superfamily members is highlighted by red circles, whereas cysteines that are specific to VISTA are marked by blue circles. The unique VISTA cysteine pattern is conserved in all orthologues from zebrafish to human.