1f11
From Proteopedia
(New page: 200px<br /> <applet load="1f11" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f11, resolution 3.0Å" /> '''F124 FAB FRAGMENT FR...) |
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| - | [[Image:1f11.gif|left|200px]]<br /> | + | [[Image:1f11.gif|left|200px]]<br /><applet load="1f11" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1f11" size=" | + | |
caption="1f11, resolution 3.0Å" /> | caption="1f11, resolution 3.0Å" /> | ||
'''F124 FAB FRAGMENT FROM A MONOCLONAL ANTI-PRES2 ANTIBODY'''<br /> | '''F124 FAB FRAGMENT FROM A MONOCLONAL ANTI-PRES2 ANTIBODY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the Fab fragment from the monoclonal anti-preS2 | + | The crystal structure of the Fab fragment from the monoclonal anti-preS2 antibody F124 (IgG1,kappa) has been solved by molecular replacement and refined at 3.0 A resolution. The Fab crystallizes with two independent molecules in the asymmetric unit. F124 recognizes an epitope contained within the preS2 segment between residues 120 and 132 of the surface antigen of hepatitis B virus. The antibody shows a high affinity for the glycan N-linked to Asn123, but it also cross-reacts with the non-glycosylated peptide fragment 120-132. Although crystallization was performed in the presence of an eightfold excess of the cross-reactive peptide, no evidence for the ligand was found in the antigen-binding site, which is close to a neighbouring molecule in the crystal lattice. The antigen-binding site has a groove-like topology which is modulated with pocket-like cavities. It is characterized by a large number of tyrosine and aspartate residues. The importance of germ-line mutations at the binding site is discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1F11 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1F11 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F11 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Bentley, G | + | [[Category: Bentley, G A.]] |
| - | [[Category: Normand, B | + | [[Category: Normand, B Vulliez-Le.]] |
[[Category: Passafiume, M.]] | [[Category: Passafiume, M.]] | ||
| - | [[Category: Riottot, M | + | [[Category: Riottot, M M.]] |
| - | [[Category: Saul, F | + | [[Category: Saul, F A.]] |
[[Category: antibody]] | [[Category: antibody]] | ||
[[Category: fab]] | [[Category: fab]] | ||
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[[Category: pres2]] | [[Category: pres2]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:39 2008'' |
Revision as of 10:33, 21 February 2008
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F124 FAB FRAGMENT FROM A MONOCLONAL ANTI-PRES2 ANTIBODY
Overview
The crystal structure of the Fab fragment from the monoclonal anti-preS2 antibody F124 (IgG1,kappa) has been solved by molecular replacement and refined at 3.0 A resolution. The Fab crystallizes with two independent molecules in the asymmetric unit. F124 recognizes an epitope contained within the preS2 segment between residues 120 and 132 of the surface antigen of hepatitis B virus. The antibody shows a high affinity for the glycan N-linked to Asn123, but it also cross-reacts with the non-glycosylated peptide fragment 120-132. Although crystallization was performed in the presence of an eightfold excess of the cross-reactive peptide, no evidence for the ligand was found in the antigen-binding site, which is close to a neighbouring molecule in the crystal lattice. The antigen-binding site has a groove-like topology which is modulated with pocket-like cavities. It is characterized by a large number of tyrosine and aspartate residues. The importance of germ-line mutations at the binding site is discussed.
About this Structure
1F11 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the Fab fragment from F124, a monoclonal antibody specific for hepatitis B surface antigen., Saul FA, Vulliez-Le Normand B, Passafiume M, Riottot MM, Bentley GA, Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):945-51. PMID:10944330
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