4pls: Difference between revisions
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==Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure.== | ==Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure.== | ||
<StructureSection load='4pls' size='340' side='right' caption='[[4pls]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='4pls' size='340' side='right'caption='[[4pls]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4pls]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PLS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PLS FirstGlance]. <br> | <table><tr><td colspan='2'>[[4pls]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PLS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PLS FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4pls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pls OCA], [http://pdbe.org/4pls PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pls RCSB], [http://www.ebi.ac.uk/pdbsum/4pls PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pls ProSAT]</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=4pls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pls OCA], [http://pdbe.org/4pls PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pls RCSB], [http://www.ebi.ac.uk/pdbsum/4pls PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pls ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct sequences]] | |||
[[Category: Madhurantakam, C]] | [[Category: Madhurantakam, C]] | ||
[[Category: Mittl, P R]] | [[Category: Mittl, P R]] | ||
Revision as of 11:01, 17 April 2019
Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure.Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure.
Structural highlights
Publication Abstract from PubMedDesigned armadillo repeat proteins (dArmRP) are promising modular proteins for the engineering of binding molecules that recognize extended polypeptide chains. We determined the structure of a dArmRP containing five internal repeats and 3rd generation capping repeats in three different states by X-ray crystallography: without N-terminal His6 -tag and in the presence of calcium (YM5 A/Ca2+ ), without N-terminal His6 -tag and in the absence of calcium (YM5 A), and with N-terminal His6 -tag and in the presence of calcium (His-YM5 A/Ca2+ ). All structures show different quaternary structures and superhelical parameters. His-YM5 A/Ca2+ forms a crystallographic dimer, which is bridged by the His6 -tag, YM5 A/Ca2+ forms a domain-swapped tetramer, and only in the absence of calcium and the His6 -tag, YM5 A forms a monomer. The changes of superhelical parameters are a consequence of calcium binding, because calcium ions interact with negatively charged residues, which can also participate in the modulation of helix dipole moments between adjacent repeats. These observations are important for further optimizations of dArmRPs and provide a general illustration of how construct design and crystallization conditions can influence the exact structure of the investigated protein. Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure.,Reichen C, Madhurantakam C, Pluckthun A, Mittl PR Protein Sci. 2014 Aug 13. doi: 10.1002/pro.2535. PMID:25132085[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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