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New page: left|200px<br /><applet load="8fab" size="350" color="white" frame="true" align="right" spinBox="true" caption="8fab, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:8fab.gif|left|200px]]<br /><applet load="8fab" size="350" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURE OF THE FAB FRAGMENT FROM THE HUMAN MYELOMA IMMUNOGLOBULIN IGG HIL AT 1.8 ANGSTROMS RESOLUTION'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE FAB FRAGMENT FROM THE HUMAN MYELOMA IMMUNOGLOBULIN IGG HIL AT 1.8 ANGSTROMS RESOLUTION==
The structure of the antigen-binding fragment (Fab) of an, anti-p-azophenylarsonate monoclonal antibody, 36-71, bearing a major, cross-reactive idiotype of A/J mice has been refined to an R factor of, 24.8% at a resolution of 1.85 A. The previously solved partial structure, of this Fab at a resolution of 2.9 A (Rose et al., 1990) was used as an, initial model for refinement against the high-resolution data. The complex, with hapten has been modeled by docking the small-molecule crystal, structure of phenylarsonic acid into the structure of the native Fab on, the basis of a low-resolution electron density map of the complex. In this, model, residue Arg-96 in the light chain and residues Asn-35, Trp-47, and, Ser-99 in the heavy chain contact the arsonate moiety of the hapten; an, additional bond is found between the arsonate group and a tightly bound, water molecule. The phenyl moiety of the hapten packs against two tyrosine, side chains at positions 50 and 106 in the heavy chain. Residue Arg-96 in, the light chain had been implicated as involved in hapten binding on the, basis of previous experiments, and indeed, this residue appears to play a, crucial role in this model. Experiments employing site-directed, mutagenesis directly support this conclusion. The heavy-chain, complementarity-determining regions have novel conformations not, previously observed in immunoglobulins except for the recently solved, anti-p-azophenylarsonate Fab R 19.9 (Lascombe et al., 1989).
<StructureSection load='8fab' size='340' side='right'caption='[[8fab]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8fab]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FAB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8fab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fab OCA], [https://pdbe.org/8fab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fab RCSB], [https://www.ebi.ac.uk/pdbsum/8fab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fab ProSAT]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/8fab_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=8fab ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of the antigen-binding fragment (Fab) of an anti-p-azophenylarsonate monoclonal antibody, 36-71, bearing a major cross-reactive idiotype of A/J mice has been refined to an R factor of 24.8% at a resolution of 1.85 A. The previously solved partial structure of this Fab at a resolution of 2.9 A (Rose et al., 1990) was used as an initial model for refinement against the high-resolution data. The complex with hapten has been modeled by docking the small-molecule crystal structure of phenylarsonic acid into the structure of the native Fab on the basis of a low-resolution electron density map of the complex. In this model, residue Arg-96 in the light chain and residues Asn-35, Trp-47, and Ser-99 in the heavy chain contact the arsonate moiety of the hapten; an additional bond is found between the arsonate group and a tightly bound water molecule. The phenyl moiety of the hapten packs against two tyrosine side chains at positions 50 and 106 in the heavy chain. Residue Arg-96 in the light chain had been implicated as involved in hapten binding on the basis of previous experiments, and indeed, this residue appears to play a crucial role in this model. Experiments employing site-directed mutagenesis directly support this conclusion. The heavy-chain complementarity-determining regions have novel conformations not previously observed in immunoglobulins except for the recently solved anti-p-azophenylarsonate Fab R 19.9 (Lascombe et al., 1989).


==About this Structure==
Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 1. X-ray crystallography, site-directed mutagenesis, and modeling of the complex with hapten.,Strong RK, Campbell R, Rose DR, Petsko GA, Sharon J, Margolies MN Biochemistry. 1991 Apr 16;30(15):3739-48. PMID:2015229<ref>PMID:2015229</ref>
8FAB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FAB OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 1. X-ray crystallography, site-directed mutagenesis, and modeling of the complex with hapten., Strong RK, Campbell R, Rose DR, Petsko GA, Sharon J, Margolies MN, Biochemistry. 1991 Apr 16;30(15):3739-48. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2015229 2015229]
</div>
<div class="pdbe-citations 8fab" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Sandbox 20009|Sandbox 20009]]
*[[3D structures of human antibody|3D structures of human antibody]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Poljak, R.J.]]
[[Category: Poljak RJ]]
[[Category: Saul, F.A.]]
[[Category: Saul FA]]
[[Category: immunoglobulin]]
 
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