32c2

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[[Image:32c2.gif|left|200px]]
 
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==STRUCTURE OF AN ACTIVITY SUPPRESSING FAB FRAGMENT TO CYTOCHROME P450 AROMATASE==
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The line below this paragraph, containing "STRUCTURE_32c2", creates the "Structure Box" on the page.
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<StructureSection load='32c2' size='340' side='right'caption='[[32c2]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[32c2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=32C2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=32C2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=32c2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=32c2 OCA], [https://pdbe.org/32c2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=32c2 RCSB], [https://www.ebi.ac.uk/pdbsum/32c2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=32c2 ProSAT]</span></td></tr>
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{{STRUCTURE_32c2| PDB=32c2 | SCENE= }}
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/2c/32c2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=32c2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of a Fab fragment (Fab3-2C2) of a monoclonal antibody raised against aromatase cytochrome P450 P450arom) has been determined at 3.0 A resolution. P450arom is a membrane bound enzyme responsible for the catalysis of indrogens to estrogens, the process of aromatization, and hence has been implicated in hormone-dependent breast cancer. The Fab fragment of MAb3-2C2 IgG suppresses P450arom activity in a dose dependent manner. The Fab3-2C2 molecule crystallizes n the space group P2(1)2(1)2(1) with a unit cell of a= 154.89 A, b = 73.51 A, and c= 36.90 A. The crystal structure consists of a light and a heavy chain in the asymmetric unit, each characterized by the greek-key antiparallel beta barrel folding seen in all Fab structures. The average elbow angle between the two domains is 143 degrees. Modeling of the interactions between the variable domains of the antibody and a known model of P450arom maps the epitope to a region of the enzyme that is consistent with the available biochemical data and the activity-suppressing function of the antibody. The epitope mapping result is further supported by the inability of MAb3-2C2 IgG to suppress the activity of, or to interact with placental porcine P450arom, which is 81% identical (86% similar) to human P450arom but has a few key substitutions in the putative epitope region.
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'''STRUCTURE OF AN ACTIVITY SUPPRESSING FAB FRAGMENT TO CYTOCHROME P450 AROMATASE'''
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Structure of an activity suppressing Fab fragment to cytochrome P450 aromatase: insights into the antibody-antigen interactions.,Sawicki MW, Ng PC, Burkhart BM, Pletnev VZ, Higashiyama T, Osawa Y, Ghosh D Mol Immunol. 1999 May;36(7):423-32. PMID:10449095<ref>PMID:10449095</ref>
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==Overview==
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The crystal structure of a Fab fragment (Fab3-2C2) of a monoclonal antibody raised against aromatase cytochrome P450 P450arom) has been determined at 3.0 A resolution. P450arom is a membrane bound enzyme responsible for the catalysis of indrogens to estrogens, the process of aromatization, and hence has been implicated in hormone-dependent breast cancer. The Fab fragment of MAb3-2C2 IgG suppresses P450arom activity in a dose dependent manner. The Fab3-2C2 molecule crystallizes n the space group P2(1)2(1)2(1) with a unit cell of a= 154.89 A, b = 73.51 A, and c= 36.90 A. The crystal structure consists of a light and a heavy chain in the asymmetric unit, each characterized by the greek-key antiparallel beta barrel folding seen in all Fab structures. The average elbow angle between the two domains is 143 degrees. Modeling of the interactions between the variable domains of the antibody and a known model of P450arom maps the epitope to a region of the enzyme that is consistent with the available biochemical data and the activity-suppressing function of the antibody. The epitope mapping result is further supported by the inability of MAb3-2C2 IgG to suppress the activity of, or to interact with placental porcine P450arom, which is 81% identical (86% similar) to human P450arom but has a few key substitutions in the putative epitope region.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=32C2 OCA].
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</div>
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<div class="pdbe-citations 32c2" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structure of an activity suppressing Fab fragment to cytochrome P450 aromatase: insights into the antibody-antigen interactions., Sawicki MW, Ng PC, Burkhart BM, Pletnev VZ, Higashiyama T, Osawa Y, Ghosh D, Mol Immunol. 1999 May;36(7):423-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10449095 10449095]
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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[[Category: Burkhart, B.]]
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== References ==
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[[Category: Ghosh, D.]]
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<references/>
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[[Category: Higashiyama, T.]]
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__TOC__
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[[Category: Ng, P C.]]
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</StructureSection>
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[[Category: Osawa, Y.]]
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[[Category: Large Structures]]
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[[Category: Pletnev, V.]]
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[[Category: Mus musculus]]
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[[Category: Sawicki, M W.]]
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[[Category: Burkhart B]]
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[[Category: Antibody]]
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[[Category: Ghosh D]]
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[[Category: Aromatase]]
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[[Category: Higashiyama T]]
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[[Category: Fab]]
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[[Category: Ng PC]]
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[[Category: P450]]
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[[Category: Osawa Y]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:15:58 2008''
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[[Category: Pletnev V]]
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[[Category: Sawicki MW]]

Current revision

STRUCTURE OF AN ACTIVITY SUPPRESSING FAB FRAGMENT TO CYTOCHROME P450 AROMATASE

PDB ID 32c2

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