1ucb: Difference between revisions
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|PDB= 1ucb |SIZE=350|CAPTION= <scene name='initialview01'>1ucb</scene>, resolution 2.5Å | |PDB= 1ucb |SIZE=350|CAPTION= <scene name='initialview01'>1ucb</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ucb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ucb OCA], [http://www.ebi.ac.uk/pdbsum/1ucb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ucb RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
The X-ray structure of the uncomplexed human chimeric Fab' of the anti-tumor antibody BR96 has been determined at 2.6 A resolution. The structure has been compared with Lewis Y antigen-complexed structures of BR96 which were determined previously. The comparison reveals segmental motions and/or conformational rearrangements of three CDR loops (L1, L3, and H2), whereas CDR H3 does not undergo changes upon complexation despite its significant main-chain contacts to the carbohydrate antigen. In light of the uncomplexed chimeric Fab' structure reported here, the previously observed high mobility of the CL:CH1 domains of the complexed chimeric BR96 Fab is rationalized as a "swinging" motion approximately about the axis of the elbow bend. | The X-ray structure of the uncomplexed human chimeric Fab' of the anti-tumor antibody BR96 has been determined at 2.6 A resolution. The structure has been compared with Lewis Y antigen-complexed structures of BR96 which were determined previously. The comparison reveals segmental motions and/or conformational rearrangements of three CDR loops (L1, L3, and H2), whereas CDR H3 does not undergo changes upon complexation despite its significant main-chain contacts to the carbohydrate antigen. In light of the uncomplexed chimeric Fab' structure reported here, the previously observed high mobility of the CL:CH1 domains of the complexed chimeric BR96 Fab is rationalized as a "swinging" motion approximately about the axis of the elbow bend. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Bajorath, J.]] | [[Category: Bajorath, J.]] | ||
[[Category: Sheriff, S.]] | [[Category: Sheriff, S.]] | ||
[[Category: anti-tumor]] | [[Category: anti-tumor]] | ||
[[Category: antibody]] | [[Category: antibody]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:08:20 2008'' | ||
Revision as of 21:08, 30 March 2008
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| 1ucb, resolution 2.5Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF UNCOMPLEXED FAB COMPARED TO COMPLEX (1CLY, 1CLZ)
Overview
The X-ray structure of the uncomplexed human chimeric Fab' of the anti-tumor antibody BR96 has been determined at 2.6 A resolution. The structure has been compared with Lewis Y antigen-complexed structures of BR96 which were determined previously. The comparison reveals segmental motions and/or conformational rearrangements of three CDR loops (L1, L3, and H2), whereas CDR H3 does not undergo changes upon complexation despite its significant main-chain contacts to the carbohydrate antigen. In light of the uncomplexed chimeric Fab' structure reported here, the previously observed high mobility of the CL:CH1 domains of the complexed chimeric BR96 Fab is rationalized as a "swinging" motion approximately about the axis of the elbow bend.
About this Structure
1UCB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
X-ray structure of the uncomplexed anti-tumor antibody BR96 and comparison with its antigen-bound form., Sheriff S, Chang CY, Jeffrey PD, Bajorath J, J Mol Biol. 1996 Jun 28;259(5):938-46. PMID:8683596
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