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. 2017 Jan 17;7:698. doi: 10.3389/fimmu.2016.00698

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Copyright © 2017 Cisneros, Estefanía and Vilches.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Comparison of the primary structures of the KIR2DL5A*001 and *005 D2 Ig-like domains, along with those of KIR2DL1 alleles *001 and *014, and KIR2DL4*001. Arrows mark KIR2DL5A polymorphic positions 152 and 174, and Phe-129, predictably confronted to Gly/Ser-174 in the receptor architecture. Other residues mentioned in the text are underlined. Amino acid numbering is based on the mature KIR2DL5A polypeptide (the KIR2DL1 N-terminal Ig-like domain, not represented, is five amino acids longer than those of killer-cell Ig-like receptors 2DL4 and 2DL5).