Skip to main content
. Author manuscript; available in PMC: 2018 Jul 5.
Published in final edited form as: Structure. 2017 Jun 22;25(7):1068–1078.e2. doi: 10.1016/j.str.2017.05.015

Figure 6. Residues of the QR interface.

Figure 6

Top: Sequence alignment of β- and γ-crystallins exhibiting the QR interface. Human βB1 (GenBank: AAC50383.1); Human βB2 (GenBank: AB25691.1); Human βA4 (GenBank: AAC50970.1) Chicken γS (GenBank: ACX94083.1). Initiator methionines are not included in alignment or numbering. Protein sequences are aligned to emphasize the common four motif structure with the important G and S residues in blue. General positions of β-strands are indicated with a, b, c, d indicating the four strands of each motif. Residues involved in the QR interface, as defined by Contact are shown colored. Sequence positions are given for βB1 (above) and γS (below). Details of contacts are listed in Table S2. Below: Only one residue is completely conserved in the different QR interfaces. A: An example of a non-polar contact in the βB1 dimer (green) that is not present in the chicken γS QR interface (red). B: Arg145 of γS (red) and Arg201 of βB1 (green) are conserved, but adopt different conformations in the two proteins. C: Tyr144 (of γS) is completely conserved in all QR interfaces. A multiple alignment of γS and β-crystallin structures with the QR interface shows the close superposition of the conserved tyrosine equivalent to Y144 in γS (Y). Colors are as in fig 5.