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your search for "cytokine" returned 37 result(s).
Hinge bending within the cytokine receptor superfamily revealed by the 2.4 Å crystal structure of the extracellular domain of rabbit tissue factor
- Published on Dec 31, 2008
Tissue factor (TF), a member of the cytokine receptor superfamily, is the obligate cofactor of coagulation factor VIIa (FVIIa), and has a pivotal role in initiating the extrinsic pathway of blood coagulation through formation of the TF-FVIIa complex. The crystal structure of the extracellular portion of rabbit TF has been solved at 2.35 Å resolution and refined to a crystallographic R-value of 19.1% (free R-value, 27.7%). Like the human homologue, the extracellular portion consists of two...
Backbone dynamics measurements on leukemia inhibitory factor, a rigid four-helical bundle cytokine
- Published on Dec 31, 2008
The backbone dynamics of the four-helical bundle cytokine leukemia inhibitory factor (LIF) have been investigated using 15N NMR relaxation and amide proton exchange measurements on a murine - human chimera, MH35-LIF. For rapid backbone motions (on a time scale of 10 ps to 100 ns), as probed by 15N relaxation measurements, the dynamics parameters were calculated using the model-free formalism incorporating the model selection approach. The principal components of the inertia tensor of MH35-LIF,...
LIF receptor-gp130 interaction investigated by homology modeling: Implications for LIF binding
- Published on Dec 31, 2008
Leukemia inhibitory factor (LIF), a member of the gpl30 family of helical cytokines, is involved in the hemopoietic and neural systems. The LIF signal transducing complex contains two receptor molecules, the LIF receptor (LIFR) and gp130. The extracellular region of the LIFR is unique in that it includes three membrane-proximal fibronectin type III domains and two cytokine binding domains (CBDs) separated by an immunoglobulin-like domain. Although some mutagenesis data on LIF are available, it...
LTHREADER: Prediction of extracellular ligand-receptor interactions in cytokines using localized threading
- Published on Jan 02, 2009
Identification of extracellular ligand-receptor interactions is important for drug design and the treatment of diseases. Difficulties in detecting these interactions using high-throughput experimental techniques motivate the development of computational prediction methods. We propose a novel threading algorithm, LTHREADER, which generates accurate local sequence-structure interface alignments and integrates various statistical scores and experimental binding data to predict interactions within...
Template-based docking of a prolactin receptor proline-rich motif octapeptide to FKBP12: Implications for cytokine receptor signaling
- Published on Dec 31, 2008
A conserved proline-rich motif (PRM) in the cytoplasmic domain of cytokine receptors has been suggested to be a signaling switch regulated by the action of the FK506 binding protein (FKBP) family of peptidylprolyl isomerases (O'Neal KD, Yu-Lee LY, Shearer WT, 1995, Ann NY Acad Sci 766:282-284). We have docked the prolactin receptor PRM (Ile1-Phe2-Pro3-Pro4-Val5-Pro6-Gly7-Pro8) to the ligand binding site of FKBP12. The procedure involved conformational search restricted by NMR restraints (O'Neal...
