5WK3
CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CCL17 AND M116 FAB
Summary for 5WK3
| Entry DOI | 10.2210/pdb5wk3/pdb |
| Descriptor | M116 LIGHT CHAIN, M116 HEAVY CHAIN, C-C motif chemokine 17, ... (5 entities in total) |
| Functional Keywords | immune system |
| Biological source | Homo sapiens (HUMAN) More |
| Cellular location | Secreted: Q92583 |
| Total number of polymer chains | 12 |
| Total formula weight | 228023.15 |
| Authors | Teplyakov, A.,Obmolova, G.,Gilliland, G.L. (deposition date: 2017-07-24, release date: 2017-12-20, Last modification date: 2024-11-13) |
| Primary citation | Teplyakov, A.,Obmolova, G.,Gilliland, G.L. Structural insights into chemokine CCL17 recognition by antibody M116. Biochem Biophys Rep, 13:27-31, 2018 Cited by PubMed Abstract: The homeostatic chemokine CCL17, also known as thymus and activation regulated chemokine (TARC), has been associated with various diseases such as asthma, idiopathic pulmonary fibrosis, atopic dermatitis and ulcerative colitis. Neutralization of CCL17 by antibody treatment ameliorates the impact of disease by blocking influx of T cells. Monoclonal antibody M116 derived from a combinatorial library shows potency in neutralizing CCL17-induced signaling. To gain insight into the structural determinants of antigen recognition, the crystal structure of M116 Fab was determined in complex with CCL17 and in the unbound form. Comparison of the structures revealed an unusual induced-fit mechanism of antigen recognition that involves isomerization in two CDRs. The structure of the CCL17-M116 complex revealed the antibody binding epitope, which does not overlap with the putative receptor epitope, suggesting that the current model of chemokine-receptor interactions, as observed in the CXCR4-vMIP-II system, may not be universal. PubMed: 29264403DOI: 10.1016/j.bbrep.2017.11.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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