4bfi

Structure of the complex of the extracellular portions of mouse CD200R and mouse CD200

spinqualitylabelsall models 4bfi, resolution 3.22Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bfi is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.22Å Ligands: CYS, EDO, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MO2R1_MOUSE Publication Abstract from PubMed CD200 is a widely distributed membrane glycoprotein that regulates myeloid cell activity through its interaction with an inhibitory receptor (CD200R). The interaction is of interest as a target for treating excessive inflammation and for treating leukemia. There are closely related proteins to CD200R that give activating signals making this a "paired receptor." We report X-ray crystallography structures for the inhibitory CD200R, the activating receptor CD200RLa, and a complex between CD200R and CD200. Both CD200 and CD200R contain two Ig-like domains and interact through their NH2 terminal domains compatible with immunological synapse-like interactions occurring between myeloid cells and other CD200-expressing cells. The failure of the activating receptor to bind CD200 resides in subtle changes around the interface. CD200 has been acquired by herpes viruses to mimic the host interaction. CD200R has evolved rapidly presumably driven by pathogen pressure but it may also be important in homeostasis through interactions with commensal bacteria. Structures of CD200/CD200 Receptor Family and Implications for Topology, Regulation, and Evolution.,Hatherley D, Lea SM, Johnson S, Barclay AN Structure. 2013 Apr 17. pii: S0969-2126(13)00090-7. doi:, 10.1016/j.str.2013.03.008. PMID:23602662 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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