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. Author manuscript; available in PMC: 2010 Jul 17.
Published in final edited form as: Circ Res. 2009 Jun 25;105(2):176–184. doi: 10.1161/CIRCRESAHA.109.200576

Figure 4.

Figure 4

Structure-function comparison of CyRP-71 with RXP-E. Top: amino acid sequence (one-letter code) of RXP-E (see also16). A: Molecular overlay of predicted spatial position for amino acids R1, R2 and R6 of CyRP-71 (green) with positively charged amino acids K29, R31 and R34 in C-end of RXP-E (red). L Spatial correlation was consistent with the ability of peptide to bind Cx43CT by SPR (panel B; peptide sequence on top; peptide concentrations as noted). C: At amino end of RXP-E, overlay of positively charged residues R5 and H10 of RXP-E (red) over R1–R2 of CyRP-71 (green) predicts that two acidic residues (D2 and D3) occupy the position held by a basic amino acid (R6) in CyRP-71. The latter would be inconsistent with occupation of the same binding pocket. D: As predicted, a peptide of the amino end of RXP-E (sequence on top of panel) failed to bind Cx43CT by SPR.