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1bln

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[[Image:1bln.gif|left|200px]]
[[Image:1bln.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1bln", creates the "Structure Box" on the page.
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{{STRUCTURE_1bln| PDB=1bln | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bln OCA], [http://www.ebi.ac.uk/pdbsum/1bln PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bln RCSB]</span>
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'''ANTI-P-GLYCOPROTEIN FAB MRK-16'''
'''ANTI-P-GLYCOPROTEIN FAB MRK-16'''
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==About this Structure==
==About this Structure==
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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].
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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://www.ncbi.nlm.nih.gov/pubmed/9738009 9738009]
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]
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[[Category: Mus musculus]]
 
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[[Category: Protein complex]]
 
[[Category: Rose, D R.]]
[[Category: Rose, D R.]]
[[Category: Tsuruo, T.]]
[[Category: Tsuruo, T.]]
[[Category: Vasudevan, S.]]
[[Category: Vasudevan, S.]]
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[[Category: immunoglobulin]]
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[[Category: Immunoglobulin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:40:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:03:30 2008''
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Revision as of 08:40, 2 May 2008

Template:STRUCTURE 1bln

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

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 Page seeded by OCA on Fri May 2 11:40:27 2008

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