1clz
From Proteopedia
(New page: 200px<br /> <applet load="1clz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1clz, resolution 2.8Å" /> '''IGG FAB (IGG3, KAPPA...) |
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| - | [[Image:1clz.gif|left|200px]]<br /> | + | [[Image:1clz.gif|left|200px]]<br /><applet load="1clz" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1clz" size=" | + | |
caption="1clz, resolution 2.8Å" /> | caption="1clz, resolution 2.8Å" /> | ||
'''IGG FAB (IGG3, KAPPA) FRAGMENT (MBR96) COMPLEXED WITH LEWIS Y NONOATE METHYL ESTER'''<br /> | '''IGG FAB (IGG3, KAPPA) FRAGMENT (MBR96) COMPLEXED WITH LEWIS Y NONOATE METHYL ESTER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of the murine BR96 Fab and its human chimera have | + | The crystal structures of the murine BR96 Fab and its human chimera have been determined in complex with the nonoate methyl ester derivative of Lewis Y (nLey) at 2.8 A and 2.5 A resolution, respectively. BR96 binds the carbohydrate in a large pocket which is formed by residues of all CDR loops except L2. The binding of the carbohydrate is mediated predominantly by aromatic residues in BR96. Analysis of the structure suggests that BR96 is capable of recognizing a structure larger than the Le(y) tetrasaccharide, providing a possible explanation for its high tumour selectivity. The structure provides a rationale for mutagenesis experiments that have resulted in BR96 CDR loop mutants with increased affinity for nLey and/or tumour cells. |
==About this Structure== | ==About this Structure== | ||
| - | 1CLZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NON as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CLZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NON:'>NON</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:29 2008'' |
Revision as of 10:07, 21 February 2008
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IGG FAB (IGG3, KAPPA) FRAGMENT (MBR96) COMPLEXED WITH LEWIS Y NONOATE METHYL ESTER
Overview
The crystal structures of the murine BR96 Fab and its human chimera have been determined in complex with the nonoate methyl ester derivative of Lewis Y (nLey) at 2.8 A and 2.5 A resolution, respectively. BR96 binds the carbohydrate in a large pocket which is formed by residues of all CDR loops except L2. The binding of the carbohydrate is mediated predominantly by aromatic residues in BR96. Analysis of the structure suggests that BR96 is capable of recognizing a structure larger than the Le(y) tetrasaccharide, providing a possible explanation for its high tumour selectivity. The structure provides a rationale for mutagenesis experiments that have resulted in BR96 CDR loop mutants with increased affinity for nLey and/or tumour cells.
About this Structure
1CLZ is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
The x-ray structure of an anti-tumour antibody in complex with antigen., Jeffrey PD, Bajorath J, Chang CY, Yelton D, Hellstrom I, Hellstrom KE, Sheriff S, Nat Struct Biol. 1995 Jun;2(6):466-71. PMID:7664109
Page seeded by OCA on Thu Feb 21 12:07:29 2008
