1oax

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:20, 21 November 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1oax.jpg|left|200px]]
 
-
<!--
+
==Fv Structure of the IgE SPE-7 in complex with acenaphthenequinone==
-
The line below this paragraph, containing "STRUCTURE_1oax", creates the "Structure Box" on the page.
+
<StructureSection load='1oax' size='340' side='right'caption='[[1oax]], [[Resolution|resolution]] 2.67&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'>[[1oax]] is a 6 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=1OAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAX 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]] 2.67&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANQ:ACENAPHTHENEQUINONE'>ANQ</scene></td></tr>
-
{{STRUCTURE_1oax| PDB=1oax | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oax OCA], [https://pdbe.org/1oax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oax RCSB], [https://www.ebi.ac.uk/pdbsum/1oax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oax ProSAT]</span></td></tr>
-
 
+
</table>
-
'''FV STRUCTURE OF THE IGE SPE-7 IN COMPLEX WITH ACENAPHTHENEQUINONE'''
+
== Evolutionary Conservation ==
-
 
+
[[Image:Consurf_key_small.gif|200px|right]]
-
 
+
Check<jmol>
-
==Overview==
+
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/1oax_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=1oax ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
A single antibody was shown to adopt different binding-site conformations and thereby bind unrelated antigens. Analysis by both x-ray crystallography and pre-steady-state kinetics revealed an equilibrium between different preexisting isomers, one of which possessed a promiscuous, low-affinity binding site for aromatic ligands, including the immunizing hapten. A subsequent induced-fit isomerization led to high-affinity complexes with a deep and narrow binding site. A protein antigen identified by repertoire selection made use of an unrelated antibody isomer with a wide, shallow binding site. Conformational diversity, whereby one sequence adopts multiple structures and multiple functions, can increase the effective size of the antibody repertoire but may also lead to autoimmunity and allergy.
A single antibody was shown to adopt different binding-site conformations and thereby bind unrelated antigens. Analysis by both x-ray crystallography and pre-steady-state kinetics revealed an equilibrium between different preexisting isomers, one of which possessed a promiscuous, low-affinity binding site for aromatic ligands, including the immunizing hapten. A subsequent induced-fit isomerization led to high-affinity complexes with a deep and narrow binding site. A protein antigen identified by repertoire selection made use of an unrelated antibody isomer with a wide, shallow binding site. Conformational diversity, whereby one sequence adopts multiple structures and multiple functions, can increase the effective size of the antibody repertoire but may also lead to autoimmunity and allergy.
-
==About this Structure==
+
Antibody multispecificity mediated by conformational diversity.,James LC, Roversi P, Tawfik DS Science. 2003 Feb 28;299(5611):1362-7. PMID:12610298<ref>PMID:12610298</ref>
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAX OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Antibody multispecificity mediated by conformational diversity., James LC, Roversi P, Tawfik DS, Science. 2003 Feb 28;299(5611):1362-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12610298 12610298]
+
</div>
-
[[Category: James, L C.]]
+
<div class="pdbe-citations 1oax" style="background-color:#fffaf0;"></div>
-
[[Category: Roversi, P.]]
+
== References ==
-
[[Category: Tawfik, D.]]
+
<references/>
-
[[Category: Allergy]]
+
__TOC__
-
[[Category: Antibody]]
+
</StructureSection>
-
[[Category: Ige]]
+
[[Category: Large Structures]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:36:47 2008''
+
[[Category: Mus musculus]]
 +
[[Category: James LC]]
 +
[[Category: Roversi P]]
 +
[[Category: Tawfik D]]

Current revision

Fv Structure of the IgE SPE-7 in complex with acenaphthenequinone

PDB ID 1oax

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oax"
Personal tools