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4BFE

Structure of the extracellular portion of mouse CD200RLa

Summary for 4BFE
Entry DOI10.2210/pdb4bfe/pdb
Related4BFG 4BFI
DescriptorCELL SURFACE GLYCOPROTEIN CD200 RECEPTOR 4, 2-acetamido-2-deoxy-beta-D-glucopyranose, CYSTEINE, ... (6 entities in total)
Functional Keywordsimmune system, paired receptor, ig domains, viral mimicry, leukaemia
Biological sourceMUS MUSCULUS (HOUSE MOUSE)
Cellular locationMembrane; Single-pass type I membrane protein (Potential): Q6XJV4
Total number of polymer chains3
Total formula weight77641.96
Authors
Hatherley, D.,Lea, S.M.,Johnson, S.,Barclay, A.N. (deposition date: 2013-03-18, release date: 2013-05-01, Last modification date: 2024-10-23)
Primary citationHatherley, D.,Lea, S.M.,Johnson, S.,Barclay, A.N.
Structures of Cd200/Cd200 Receptor Family and Implications for Topology, Regulation, and Evolution
Structure, 21:820-, 2013
Cited by
PubMed Abstract: 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.
PubMed: 23602662
DOI: 10.1016/J.STR.2013.03.008
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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