1clz
From Proteopedia
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|PDB= 1clz |SIZE=350|CAPTION= <scene name='initialview01'>1clz</scene>, resolution 2.8Å | |PDB= 1clz |SIZE=350|CAPTION= <scene name='initialview01'>1clz</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NON:METHYL NONANOATE (ESTER)'>NON</scene> | + | |LIGAND= <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NON:METHYL+NONANOATE+(ESTER)'>NON</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1clz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1clz OCA], [http://www.ebi.ac.uk/pdbsum/1clz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1clz RCSB]</span> | ||
}} | }} | ||
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[[Category: Bajorath, J.]] | [[Category: Bajorath, J.]] | ||
[[Category: Sheriff, S.]] | [[Category: Sheriff, S.]] | ||
| - | [[Category: NON]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
[[Category: immunoglobulin c region]] | [[Category: immunoglobulin c region]] | ||
[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:13 2008'' |
Revision as of 16:24, 30 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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