2a9n: Difference between revisions
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<StructureSection load='2a9n' size='340' side='right' caption='[[2a9n]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='2a9n' size='340' side='right' caption='[[2a9n]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2a9n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2a9n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A9N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A9N FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ORE:4-(2,7-DIFLUORO-6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)ISOPHTHALIC+ACID'>ORE</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ORE:4-(2,7-DIFLUORO-6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)ISOPHTHALIC+ACID'>ORE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a9m|2a9m]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a9m|2a9m]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a9n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2a9n RCSB], [http://www.ebi.ac.uk/pdbsum/2a9n PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a9n OCA], [http://pdbe.org/2a9n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a9n RCSB], [http://www.ebi.ac.uk/pdbsum/2a9n PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2a9n" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Cambillau, C]] | [[Category: Cambillau, C]] | ||
[[Category: Honegger, A]] | [[Category: Honegger, A]] | ||
Revision as of 20:33, 11 September 2015
A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of a Tight-binding Fluorescein-scFv complexA Mutation Designed to Alter Crystal Packing Permits Structural Analysis of a Tight-binding Fluorescein-scFv complex
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 structure of the scFv fragment FITC-E2, obtained from a naive phage antibody scFv library derived from human donors, was determined at 2.1 A resolution in the free form and at 3.0 A in the complexed form. The wild-type (wt) scFv binds fluorescein with a K(D) of 0.75 nM. The free scFv readily crystallizes by compacting its 18 amino acid-long CDR-H3, partially occluding the binding site and further blocking access by binding to the "bottom" of a neighboring scFv molecule with a cluster of exposed aromatic residues within CDR-H3. Only upon mutating one of the residues involved in this dominant crystal contact, an exposed tryptophan in the middle of CDR-H3, crystals of the complex could be obtained. A series of alanine mutants within the putative antigen binding site, covering a range of binding affinities, were used to relate macroscopic thermodynamic and kinetic binding parameters to single-molecule disruption forces measured by AFM. The effects of the mutations on the binding properties, particularly on the fraction of binding-competent molecules within the population, cannot be fully explained by changes in the strength of local interactions. The significant conformational change of CDR-H3 between the free and the liganded form illustrates the plasticity of the binding site. An accompanying study in this issue by Curcio and colleagues presents the molecular dynamics simulation of the forced unbinding experiments and explores possible effects of the mutations on the unbinding pathway of the hapten. A mutation designed to alter crystal packing permits structural analysis of a tight-binding fluorescein-scFv complex.,Honegger A, Spinelli S, Cambillau C, Pluckthun A Protein Sci. 2005 Oct;14(10):2537-49. PMID:16195545[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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