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. Author manuscript; available in PMC: 2013 Jan 1.
Published in final edited form as: Mol Immunol. 2011 Dec 12;49(4):628–639. doi: 10.1016/j.molimm.2011.11.002

Figure 1. Location of tapasin residues involved in MHC class I association.

Figure 1

(A) Tapasin residues 334-342 (shown in orange) lie on a loop within the C-terminal Ig-like domain. Also, shown in blue are residues within the N-terminal Ig-like domain which were proposed to comprise a binding site for the MHC class I α2-1 helix (Dong et al., 2009). The ribbon diagram was generated from an x-ray crystallographic structure of the tapasin/ERp57 heterodimer (Dong et al., 2009) (PDB code 3F8U) using PyMOL (Schrödinger, 2010). (B) Deletion of residues 334-342 is not predicted to alter the overall tapasin structure. Residues 334-342 were removed from the tapasin crystal structure, and the resulting structure was subjected to energy minimization as described in the Materials and methods. Amino acid residues involved in MHC class I binding are colored as in (A). Residues 333 and 343, flanking the deleted sequence, are shown in orange.