6ayz

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m (Protected "6ayz" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6ayz is ON HOLD
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==Crystal structure of Asf1-Fab 12E complex==
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<StructureSection load='6ayz' size='340' side='right' caption='[[6ayz]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6ayz]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AYZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AYZ FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uea|5uea]]</td></tr>
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<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=6ayz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ayz OCA], [http://pdbe.org/6ayz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ayz RCSB], [http://www.ebi.ac.uk/pdbsum/6ayz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ayz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ASF1_YEAST ASF1_YEAST]] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Facilitates histone deposition through both replication-dependent and replication-independent chromatin assembly pathways. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with the HIR complex to promote replication-independent chromatin assembly, which may occur during transcription and DNA repair. May be required for the maintenance of a subset of replication elongation factors, including DNA polymerase epsilon, the RFC complex and PCNA, at stalled replication forks. Also required for acetylation of histone H3 on 'Lys-9' and 'Lys-56'.<ref>PMID:9290207</ref> <ref>PMID:10591219</ref> <ref>PMID:11412995</ref> <ref>PMID:11331602</ref> <ref>PMID:11731479</ref> <ref>PMID:11731480</ref> <ref>PMID:11404324</ref> <ref>PMID:11172707</ref> <ref>PMID:11856374</ref> <ref>PMID:11756556</ref> <ref>PMID:12093919</ref> <ref>PMID:14585955</ref> <ref>PMID:15071494</ref> <ref>PMID:15452122</ref> <ref>PMID:15175160</ref> <ref>PMID:15542829</ref> <ref>PMID:15542840</ref> <ref>PMID:15766286</ref> <ref>PMID:16303565</ref> <ref>PMID:15821127</ref> <ref>PMID:15901673</ref> <ref>PMID:16020781</ref> <ref>PMID:16143623</ref> <ref>PMID:16039596</ref> <ref>PMID:15632066</ref> <ref>PMID:15891116</ref> <ref>PMID:16141196</ref> <ref>PMID:15840725</ref> <ref>PMID:16815704</ref> <ref>PMID:16936140</ref> <ref>PMID:16582440</ref> <ref>PMID:16407267</ref> <ref>PMID:17046836</ref> <ref>PMID:16678113</ref> <ref>PMID:16501045</ref> <ref>PMID:16627621</ref> <ref>PMID:17107956</ref> <ref>PMID:17320445</ref> <ref>PMID:14680630</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Antibody Fab fragments have been exploited with significant success to facilitate the structure determination of challenging macromolecules as crystallization chaperones and as molecular fiducial marks for single particle cryo-electron microscopy approaches. However, the inherent flexibility of the "elbow" regions, which link the constant and variable domains of the Fab, can introduce disorder and thus diminish their effectiveness. We have developed a phage display engineering strategy to generate synthetic Fab variants that significantly reduces elbow flexibility, while maintaining their high affinity and stability. This strategy was validated using previously recalcitrant Fab-antigen complexes where introduction of an engineered elbow region enhanced crystallization and diffraction resolution. Furthermore, incorporation of the mutations appears to be generally portable to other synthetic antibodies and may serve as a universal strategy to enhance the success rates of Fabs as structure determination chaperones.
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Authors: Bailey, L.J., Kossiakoff, A.A.
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Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination.,Bailey LJ, Sheehy KM, Dominik PK, Liang WG, Rui H, Clark M, Jaskolowski M, Kim Y, Deneka D, Tang WJ, Kossiakoff AA J Mol Biol. 2017 Dec 19. pii: S0022-2836(17)30593-4. doi:, 10.1016/j.jmb.2017.12.012. PMID:29273204<ref>PMID:29273204</ref>
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Description: Crystal structure of Asf1-Fab 12E complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Bailey, L.J]]
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<div class="pdbe-citations 6ayz" style="background-color:#fffaf0;"></div>
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[[Category: Kossiakoff, A.A]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bailey, L J]]
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[[Category: Kossiakoff, A A]]
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[[Category: Antibody]]
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[[Category: Asf1]]
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[[Category: Complex]]
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[[Category: Crystal chaperone]]
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[[Category: Immune system]]

Revision as of 06:59, 17 January 2018

Crystal structure of Asf1-Fab 12E complex

6ayz, resolution 2.10Å

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