Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.91
Classification:CYTOKINE
Release Date:2015-06-10
Deposition Date:2014-12-28
Revision Date:2015-07-01#2017-09-20
Molecular Weight:36505.6
Macromolecule Type:Protein
Residue Count:314
Atom Site Count:2539
DOI:10.2210/pdb4xfs/pdb
Abstract:
Interleukin-18 (IL-18) is a pleiotropic pro-inflammatory cytokine belonging to the IL-1 superfamily. IL-18 plays an important role in host innate and acquired immune defense, with its activity being modulated in vivo by its naturally occurring antagonist IL-18 binding protein (IL-18BP). Recent crystal structures of human IL-18 (hIL-18) in complex with its antagonist or cognate receptor(s) have revealed a conserved binding interface on hIL-18 representing a promising drug target. An important step in this process is obtaining crystals of apo hIL-18 or hIL-18 in complex with small-molecule inhibitors, preferably under low ionic strength conditions. In this study, surface-entropy reduction (SER) and rational protein design were employed to facilitate the crystallization of hIL-18. The results provide an excellent platform for structure-based drug design.
Resolution:1.91
Classification:CYTOKINE
Release Date:2015-06-10
Deposition Date:2014-12-28
Revision Date:2015-07-01#2017-09-20
Molecular Weight:36505.6
Macromolecule Type:Protein
Residue Count:314
Atom Site Count:2539
DOI:10.2210/pdb4xfs/pdb
Abstract:
Interleukin-18 (IL-18) is a pleiotropic pro-inflammatory cytokine belonging to the IL-1 superfamily. IL-18 plays an important role in host innate and acquired immune defense, with its activity being modulated in vivo by its naturally occurring antagonist IL-18 binding protein (IL-18BP). Recent crystal structures of human IL-18 (hIL-18) in complex with its antagonist or cognate receptor(s) have revealed a conserved binding interface on hIL-18 representing a promising drug target. An important step in this process is obtaining crystals of apo hIL-18 or hIL-18 in complex with small-molecule inhibitors, preferably under low ionic strength conditions. In this study, surface-entropy reduction (SER) and rational protein design were employed to facilitate the crystallization of hIL-18. The results provide an excellent platform for structure-based drug design.
| Date made available | 2015 |
|---|---|
| Publisher | RCSB-PDB |