2qhr

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(New page: 200px<br /><applet load="2qhr" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qhr, resolution 2.00&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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13F6-1-2 is a murine monoclonal antibody that recognizes the heavily, glycosylated mucin-like domain of the Ebola virus virion-attached, glycoprotein (GP) and protects animals against lethal viral challenge., Here we present the crystal structure, at 2.0 A, of 13F6-1-2 in complex, with its Ebola virus GP peptide epitope. The GP peptide binds in an, extended conformation, anchored primarily by interactions with the heavy, chain. Two GP residues, Gln P406 and Arg P409, make extensive side-chain, hydrogen bond and electrostatic interactions with the antibody and are, likely critical for recognition and affinity. The 13F6-1-2 antibody, utilizes a rare V lambda(x) light chain. The three light-chain, complementarity-determining regions do not adopt canonical conformations, and represent new classes of structures distinct from V kappa and other V, lambda light chains. In addition, although V lambda(x) had been thought to, confer specificity, all light-chain contacts are mediated through, germ-line-encoded residues. This structure of an antibody that protects, against the Ebola virus now provides a framework for humanization and, development of a postexposure immunotherapeutic.
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13F6-1-2 is a murine monoclonal antibody that recognizes the heavily glycosylated mucin-like domain of the Ebola virus virion-attached glycoprotein (GP) and protects animals against lethal viral challenge. Here we present the crystal structure, at 2.0 A, of 13F6-1-2 in complex with its Ebola virus GP peptide epitope. The GP peptide binds in an extended conformation, anchored primarily by interactions with the heavy chain. Two GP residues, Gln P406 and Arg P409, make extensive side-chain hydrogen bond and electrostatic interactions with the antibody and are likely critical for recognition and affinity. The 13F6-1-2 antibody utilizes a rare V lambda(x) light chain. The three light-chain complementarity-determining regions do not adopt canonical conformations and represent new classes of structures distinct from V kappa and other V lambda light chains. In addition, although V lambda(x) had been thought to confer specificity, all light-chain contacts are mediated through germ-line-encoded residues. This structure of an antibody that protects against the Ebola virus now provides a framework for humanization and development of a postexposure immunotherapeutic.
==About this Structure==
==About this Structure==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Abelson, D.M.]]
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[[Category: Abelson, D M.]]
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[[Category: Fusco, M.L.]]
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[[Category: Fusco, M L.]]
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[[Category: Hart, M.K.]]
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[[Category: Hart, M K.]]
[[Category: Kuehne, A.]]
[[Category: Kuehne, A.]]
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[[Category: Lee, J.E.]]
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[[Category: Lee, J E.]]
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[[Category: Saphire, E.O.]]
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[[Category: Saphire, E O.]]
[[Category: antibody-peptide complex]]
[[Category: antibody-peptide complex]]
[[Category: immune system/viral protein complex]]
[[Category: immune system/viral protein complex]]
[[Category: immunologlobulin fold]]
[[Category: immunologlobulin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:52:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:39:28 2008''

Revision as of 16:39, 21 February 2008


2qhr, resolution 2.00Å

Drag the structure with the mouse to rotate

Crystal structure of the 13F6-1-2 Fab fragment bound to its Ebola virus glycoprotein peptide epitope.

Overview

13F6-1-2 is a murine monoclonal antibody that recognizes the heavily glycosylated mucin-like domain of the Ebola virus virion-attached glycoprotein (GP) and protects animals against lethal viral challenge. Here we present the crystal structure, at 2.0 A, of 13F6-1-2 in complex with its Ebola virus GP peptide epitope. The GP peptide binds in an extended conformation, anchored primarily by interactions with the heavy chain. Two GP residues, Gln P406 and Arg P409, make extensive side-chain hydrogen bond and electrostatic interactions with the antibody and are likely critical for recognition and affinity. The 13F6-1-2 antibody utilizes a rare V lambda(x) light chain. The three light-chain complementarity-determining regions do not adopt canonical conformations and represent new classes of structures distinct from V kappa and other V lambda light chains. In addition, although V lambda(x) had been thought to confer specificity, all light-chain contacts are mediated through germ-line-encoded residues. This structure of an antibody that protects against the Ebola virus now provides a framework for humanization and development of a postexposure immunotherapeutic.

About this Structure

2QHR is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Complex of a protective antibody with its Ebola virus GP peptide epitope: unusual features of a V lambda x light chain., Lee JE, Kuehne A, Abelson DM, Fusco ML, Hart MK, Saphire EO, J Mol Biol. 2008 Jan 4;375(1):202-16. Epub 2007 Oct 16. PMID:18005986

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