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1ly2
From Proteopedia
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| , resolution 1.80Å | |||||||
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| Ligands: | |||||||
| Gene: | CR2 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of unliganded human CD21 SCR1-SCR2 (Complement receptor type 2)
Contents |
Overview
Human complement receptor type 2 (CD21) is the cellular receptor for Epstein-Barr virus (EBV), a human tumor virus. The N-terminal two short consensus repeats (SCR1-SCR2) of the receptor interact with the EBV glycoprotein gp350/220 and also with the natural CD21 ligand C3d. Here we present the crystal structure of the CD21 SCR1-SCR2 fragment in the absence of ligand and demonstrate that it is able to bind EBV. Based on a functional analysis of wild-type and mutant CD21 and molecular modeling, we identify a likely region for EBV attachment and demonstrate that this region is not involved in the interaction with C3d. A comparison with the previously determined structure of CD21 SCR1-SCR2 in complex with C3d shows that, in both cases, CD21 assumes compact V-shaped conformations. However, our analysis reveals a surprising degree of flexibility at the SCR1-SCR2 interface, suggesting interactions between the two domains are not specific. We present evidence that the V-shaped conformation is induced by deglycosylation of the protein, and that physiologic glycosylation of CD21 would result in a more extended conformation, perhaps with additional epitopes for C3d binding.
Disease
Known disease associated with this structure: Systemic lupus erythematosus, susceptibility to, 9 OMIM:[120650]
About this Structure
1LY2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of human CD21: Implications for Epstein-Barr virus and C3d binding., Prota AE, Sage DR, Stehle T, Fingeroth JD, Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10641-6. Epub 2002 Jul 16. PMID:12122212
Page seeded by OCA on Sun Mar 30 22:08:46 2008
