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New page: left|200px<br /> <applet load="1mie" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mie, resolution 1.95Å" /> '''Crystal Structure O... |
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== | ==Crystal Structure Of The Fab Fragment of Esterolytic Antibody MS5-393== | ||
The crystal structures of four related Fab fragments of a family of | <StructureSection load='1mie' size='340' side='right'caption='[[1mie]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1mie]] 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=1MIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MIE 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]] 1.95Å</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=1mie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mie OCA], [https://pdbe.org/1mie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mie RCSB], [https://www.ebi.ac.uk/pdbsum/1mie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mie 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/mi/1mie_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=1mie ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structures of four related Fab fragments of a family of catalytic antibodies displaying differential levels of esterase activity have been solved in the presence and in the absence of the transition-state analogue (TSA) that was used to elicit the immune response. The electron density maps show that the TSA conformation is essentially identical, with limited changes on hapten binding. Interactions with the TSA explain the specificity for the D rather than the L-isomer of the substrate. Differences in the residues in the hapten-binding pocket, which increase hydrophobicity, appear to correlate with an increase in the affinity of the antibodies for their substrate. Analysis of the structures at the active site reveals a network of conserved hydrogen bond contacts between the TSA and the antibodies, and points to a critical role of two conserved residues, HisL91 and LysH95, in catalysis. However, these two key residues are set into very different contexts in their respective structures, with an apparent direct correlation between the catalytic power of the antibodies and the complexity of their interactions with the rest of the protein. This suggests that the catalytic efficiency may be controlled by contacts arising from a second sphere of residues at the periphery of the active site. | |||
High-resolution crystal structure of the Fab-fragments of a family of mouse catalytic antibodies with esterase activity.,Ruzheinikov SN, Muranova TA, Sedelnikova SE, Partridge LJ, Blackburn GM, Murray IA, Kakinuma H, Takahashi-Ando N, Shimazaki K, Sun J, Nishi Y, Rice DW J Mol Biol. 2003 Sep 12;332(2):423-35. PMID:12948492<ref>PMID:12948492</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1mie" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Blackburn GM]] | |||
[[Category: Blackburn | [[Category: Kakinuma H]] | ||
[[Category: Kakinuma | [[Category: Muranova TA]] | ||
[[Category: Muranova | [[Category: Murray IA]] | ||
[[Category: Murray | [[Category: Nishi Y]] | ||
[[Category: Nishi | [[Category: Partridge LJ]] | ||
[[Category: Partridge | [[Category: Rice DW]] | ||
[[Category: Rice | [[Category: Ruzheinikov SN]] | ||
[[Category: Ruzheinikov | [[Category: Sedelnikova SE]] | ||
[[Category: Sedelnikova | [[Category: Shimazaki K]] | ||
[[Category: Shimazaki | [[Category: Sun J]] | ||
[[Category: Sun | [[Category: Takashi N]] | ||
[[Category: Takashi | |||
Latest revision as of 10:01, 30 October 2024
Crystal Structure Of The Fab Fragment of Esterolytic Antibody MS5-393Crystal Structure Of The Fab Fragment of Esterolytic Antibody MS5-393
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structures of four related Fab fragments of a family of catalytic antibodies displaying differential levels of esterase activity have been solved in the presence and in the absence of the transition-state analogue (TSA) that was used to elicit the immune response. The electron density maps show that the TSA conformation is essentially identical, with limited changes on hapten binding. Interactions with the TSA explain the specificity for the D rather than the L-isomer of the substrate. Differences in the residues in the hapten-binding pocket, which increase hydrophobicity, appear to correlate with an increase in the affinity of the antibodies for their substrate. Analysis of the structures at the active site reveals a network of conserved hydrogen bond contacts between the TSA and the antibodies, and points to a critical role of two conserved residues, HisL91 and LysH95, in catalysis. However, these two key residues are set into very different contexts in their respective structures, with an apparent direct correlation between the catalytic power of the antibodies and the complexity of their interactions with the rest of the protein. This suggests that the catalytic efficiency may be controlled by contacts arising from a second sphere of residues at the periphery of the active site. High-resolution crystal structure of the Fab-fragments of a family of mouse catalytic antibodies with esterase activity.,Ruzheinikov SN, Muranova TA, Sedelnikova SE, Partridge LJ, Blackburn GM, Murray IA, Kakinuma H, Takahashi-Ando N, Shimazaki K, Sun J, Nishi Y, Rice DW J Mol Biol. 2003 Sep 12;332(2):423-35. PMID:12948492[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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