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. Author manuscript; available in PMC: 2017 Dec 1.
Published in final edited form as: Mol Immunol. 2016 Nov 5;80:41–49. doi: 10.1016/j.molimm.2016.10.012

Figure 5. Superimposition of IINFEKL and His6-peptide structures bound by the ERAP1 regulatory domain.

Figure 5

The two complex structures with IINFEKL peptide and His6-peptide are superimposed by all the main-chain atoms of the ERAP1 regulatory domains (408 residues). Bound peptides are shown as thick stick models, while side chains of selected ERAP1 residues are shown as skinny stick models. Atoms are colored by atom types: gold for carbons of IINFEKL complex, cyan for carbons of His6 complex, blue for nitrogens, red for oxygens, and cyan sphere for a bound water molecule in the His6 complex. From left to right, the last four residues of the IINFEKL peptide are labeled in gold (PC-3 to PC), whereas to fill the same space in the His6 complex only three residues of the peptide are labeled in cyan (PC-2 to PC) plus a water molecule (Wat). Note the different locations and orientations of the carboxyl ends (PC) for these two peptides. Side chains of ERAP1 are labeled in black. Dotted lines represent hydrogen-bond interactions.