1. Binding Affinity and Interaction of LL-37 with HLA-C
Binding Affinity and Interaction of LL-37 with HLA-C*06:02 in Psoriasis 
Tomotaka Mabuchi, Noriaki Hirayama 
Journal of Investigative Dermatology 
Volume 136, Issue 9, Pages (September 2016)
DOI: /j.jid
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2. Figure 1
The binding mode between a 9-mer peptide derived from LL-37 and the HLA-C*06:02 molecule. The alpha helix and the beta strand of the HLA-C*06:02 molecule are shown in red and yellow ribbons, respectively. (a) The residues at the third, fifth, and sixth positions of the 9-mer peptide #3 (RIKDFLRNL) are depicted by space-filling models and other residues by ball-and-stick models. Carbon atoms and bonds of the third, fifth, and sixth residues are colored in cyan, yellow, and green, respectively. Other carbon atoms and bonds are colored in white. (b) The residues at the third, fifth, and sixth positions of the 9-mer peptides #3, #4, and #22 depicted by ball-and-stick models are colored in cyan, yellow, and green, respectively. Other residues are omitted for clarity. (c) The residues at the third, fifth, and sixth positions of the 9-mer peptides #9 and #12 depicted by ball-and-stick models are colored in yellow, cyan, and green, respectively. Other residues are omitted for clarity. In all figures, the basic residue is shown in cyan and the hydrophobic residues are shown in yellow or green. The approaching direction of the TCR is indicated by an arrow. TCR, T-cell receptor.
Journal of Investigative Dermatology  , DOI: ( /j.jid )
Copyright © 2016 The Authors Terms and Conditions