4plq
From Proteopedia
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| - | ''' | + | ==Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure.== |
| + | <StructureSection load='4plq' size='340' side='right' caption='[[4plq]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4plq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PLQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PLQ FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4plq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4plq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4plq RCSB], [http://www.ebi.ac.uk/pdbsum/4plq PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Designed 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<ref>PMID:25132085</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Madhurantakam, C.]] | ||
| + | [[Category: Mittl, P R.]] | ||
| + | [[Category: Pluckthun, A.]] | ||
| + | [[Category: Reichen, C.]] | ||
| + | [[Category: Designed armadillo repeat protein]] | ||
| + | [[Category: Peptide binding protein]] | ||
| + | [[Category: Protein engineering]] | ||
Revision as of 08:45, 27 August 2014
Crystal Structures of Designed Armadillo Repeat Proteins: Implications of Construct Design and Crystallization Conditions on Overall Structure.
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