View source for 5ts4


==Crystal structure of a de novo designed protein with curved beta-sheet==
<StructureSection load='5ts4' size='340' side='right'caption='[[5ts4]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ts4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TS4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.005&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ts4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ts4 OCA], [https://pdbe.org/5ts4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ts4 RCSB], [https://www.ebi.ac.uk/pdbsum/5ts4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ts4 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Active sites and ligand-binding cavities in native proteins are often formed by curved beta sheets, and the ability to control beta-sheet curvature would allow design of binding proteins with cavities customized to specific ligands. Toward this end, we investigated the mechanisms controlling beta-sheet curvature by studying the geometry of beta sheets in naturally occurring protein structures and folding simulations. The principles emerging from this analysis were used to design, de novo, a series of proteins with curved beta sheets topped with alpha helices. Nuclear magnetic resonance and crystal structures of the designs closely match the computational models, showing that beta-sheet curvature can be controlled with atomic-level accuracy. Our approach enables the design of proteins with cavities and provides a route to custom design ligand-binding and catalytic sites.

Principles for designing proteins with cavities formed by curved beta sheets.,Marcos E, Basanta B, Chidyausiku TM, Tang Y, Oberdorfer G, Liu G, Swapna GV, Guan R, Silva DA, Dou J, Pereira JH, Xiao R, Sankaran B, Zwart PH, Montelione GT, Baker D Science. 2017 Jan 13;355(6321):201-206. doi: 10.1126/science.aah7389. PMID:28082595<ref>PMID:28082595</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Baker D]]
[[Category: Basanta B]]
[[Category: Chidyausiku TM]]
[[Category: Marcos E]]
[[Category: Oberdorfer G]]
[[Category: Pereira JH]]
[[Category: Sankaran B]]
[[Category: Zwart PH]]