1bln
From Proteopedia
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| - | [[Image:1bln.gif|left|200px]] | + | [[Image:1bln.gif|left|200px]] |
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| - | '''ANTI-P-GLYCOPROTEIN FAB MRK-16''' | + | {{Structure |
| + | |PDB= 1bln |SIZE=350|CAPTION= <scene name='initialview01'>1bln</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''ANTI-P-GLYCOPROTEIN FAB MRK-16''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BLN is a [ | + | 1BLN is a [[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=1BLN OCA]. |
==Reference== | ==Reference== | ||
| - | Mode of binding of anti-P-glycoprotein antibody MRK-16 to its antigen. A crystallographic and molecular modeling study., Vasudevan S, Tsuruo T, Rose DR, J Biol Chem. 1998 Sep 25;273(39):25413-9. PMID:[http:// | + | Mode of binding of anti-P-glycoprotein antibody MRK-16 to its antigen. A crystallographic and molecular modeling study., Vasudevan S, Tsuruo T, Rose DR, J Biol Chem. 1998 Sep 25;273(39):25413-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9738009 9738009] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:12:43 2008'' |
Revision as of 08:12, 20 March 2008
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| , resolution 2.8Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
ANTI-P-GLYCOPROTEIN FAB MRK-16
Overview
Monoclonal antibody MRK-16 recognizes a discontinuous extracellular epitope on the multidrug resistance-associated ATP-binding cassette transporter, P-glycoprotein. The atomic basis for specificity of this antibody is of interest because of its potential as a modulator of P-glycoprotein activity. The crystal structure of Fab MRK-16 is reported to a resolution of 2.8 A. A structure for a portion of the epitope was derived by comparison to regions of solved structures with similar primary sequence. This has permitted a proposal for the mode of binding of the peptide epitope to the antibody, in which the peptide makes specific contacts with complementarity-determining regions H1, H2, and H3 from the heavy chain and L3 from the light chain. These interactions are consistent with epitope mapping studies and with the observation that MRK-16 is specific for human class I P-glycoprotein. This result identifies side chains in MRK-16 that would be amenable to alteration in antibody engineering experiments to derive improved multidrug resistance inhibitors for clinical use during chemotherapy. In particular, Arg-H97 contacts both Glu-746 and Asp-744 of the peptide, Arg-L96 contacts Asp-743, and Thr-H33 interacts with Thr-747. All of these epitope residues were implicated in mediating specificity by epitope mapping studies.
About this Structure
1BLN is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Mode of binding of anti-P-glycoprotein antibody MRK-16 to its antigen. A crystallographic and molecular modeling study., Vasudevan S, Tsuruo T, Rose DR, J Biol Chem. 1998 Sep 25;273(39):25413-9. PMID:9738009
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