3e8u: Difference between revisions

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-{{Seed}}
-[[Image:3e8u.jpg|left|200px]]
-<!--
+==Crystal structure and thermodynamic analysis of diagnostic Fab 106.3 complexed with BNP 5-13 (C10A) reveal basis of selective molecular recognition==
-The line below this paragraph, containing "STRUCTURE_3e8u", creates the "Structure Box" on the page.
+<StructureSection load='3e8u' size='340' side='right'caption='[[3e8u]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3e8u]] is a 3 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=3E8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E8U FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#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=3e8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e8u OCA], [https://pdbe.org/3e8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e8u RCSB], [https://www.ebi.ac.uk/pdbsum/3e8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e8u ProSAT]</span></td></tr>
-{{STRUCTURE_3e8u|  PDB=3e8u  |  SCENE=  }}
+</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/e8/3e8u_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=3e8u ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+B-type natriuretic peptide (BNP) is a naturally secreted regulatory hormone that influences blood pressure and vascular water retention in human physiology. The plasma BNP concentration is a clinically recognized biomarker for various cardiovascular diseases. Quantitative detection of BNP can be achieved in immunoassays using the high-affinity monoclonal IgG1 antibody 106.3, which binds an epitope spanning residues 5-13 of the mature bioactive peptide. To understand the structural basis of this molecular recognition, we crystallized the Fab fragment complexed with the peptide epitope and determined the three-dimensional structure by X-ray diffraction to 2.1 A resolution. The structure reveals the detailed interactions that five of the complementarity-determining regions make with the partially folded peptide. Thermodynamic measurements using fluorescence spectroscopy suggest that the interaction is enthalpy driven, with an overall change in free energy of binding, DeltaG = -54 kJ/mol, at room temperature. The parameters are interpreted on the basis of the structural information. The kinetics of binding suggest a diffusion-limited mechanism, whereby the peptide easily adopts a bound conformation upon interaction with the antibody. Moreover, comparative analysis with alanine-scanning results of the epitope explains the basis of selectivity for BNP over other related natriuretic peptides.
-===Crystal structure and thermodynamic analysis of diagnostic Fab 106.3 complexed with BNP 5-13 (C10A) reveal basis of selective molecular recognition===
+Crystal structure and thermodynamic analysis of diagnostic mAb 106.3 complexed with BNP 5-13 (C10A).,Longenecker KL, Ruan Q, Fry EH, Saldana SC, Brophy SE, Richardson PL, Tetin SY Proteins. 2009 Aug 15;76(3):536-47. PMID:19274732<ref>PMID:19274732</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3e8u" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19274732}}, adds the Publication Abstract to the page
+*[[Antibody 3D structures|Antibody 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19274732 is the PubMed ID number.
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
--->
+*[[3D structures of non-human antibody|3D structures of non-human antibody]]
-{{ABSTRACT_PUBMED_19274732}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-E8U is a 3 chains 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=3E8U OCA].
+</StructureSection>
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:19274732</ref><references group="xtra"/>
 [[Category: Mus musculus]]
-[[Category: Brophy, S E.]]
+[[Category: Brophy SE]]
-[[Category: Fry, E H.]]
+[[Category: Fry EH]]
-[[Category: Longenecker, K L.]]
+[[Category: Longenecker KL]]
-[[Category: Richardson, P L.]]
+[[Category: Richardson PL]]
-[[Category: Ruan, Q.]]
+[[Category: Ruan Q]]
-[[Category: Saldana, S S.]]
+[[Category: Saldana SS]]
-[[Category: Tetin, S Y.]]
+[[Category: Tetin SY]]
-[[Category: Fab 106 3]]
-[[Category: Igg1]]
-[[Category: Immune system]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  8 09:33:01 2009''