1ly2

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==Overview==
==Overview==
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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.
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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==
==Disease==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Fingeroth, J.D.]]
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[[Category: Fingeroth, J D.]]
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[[Category: Prota, A.E.]]
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[[Category: Prota, A E.]]
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[[Category: Sage, D.R.]]
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[[Category: Sage, D R.]]
[[Category: Stehle, T.]]
[[Category: Stehle, T.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: complement receptor; epstein barr virus; regulator of complement activation; short consensus repeat; viral receptor; complement control protein]]
[[Category: complement receptor; epstein barr virus; regulator of complement activation; short consensus repeat; viral receptor; complement control protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:21:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:30 2008''

Revision as of 11:49, 21 February 2008


1ly2, resolution 1.80Å

Drag the structure with the mouse to rotate

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 diseases 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 with as ligand. 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

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