6e5c

<StructureSection load='6e5c' size='340' side='right' caption='[[6e5c]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[6e5c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E5C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E5C FirstGlance]. <br>

</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=6e5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e5c OCA], [http://pdbe.org/6e5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e5c RCSB], [http://www.ebi.ac.uk/pdbsum/6e5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e5c ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

beta-sheet proteins carry out critical functions in biology, and hence are attractive scaffolds for computational protein design. Despite this potential, de novo design of all-beta-sheet proteins from first principles lags far behind the design of all-alpha or mixed-alphabeta domains owing to their non-local nature and the tendency of exposed beta-strand edges to aggregate. Through study of loops connecting unpaired beta-strands (beta-arches), we have identified a series of structural relationships between loop geometry, side chain directionality and beta-strand length that arise from hydrogen bonding and packing constraints on regular beta-sheet structures. We use these rules to de novo design jellyroll structures with double-stranded beta-helices formed by eight antiparallel beta-strands. The nuclear magnetic resonance structure of a hyperthermostable design closely matched the computational model, demonstrating accurate control over the beta-sheet structure and loop geometry. Our results open the door to the design of a broad range of non-local beta-sheet protein structures.

De novo design of a non-local beta-sheet protein with high stability and accuracy.,Marcos E, Chidyausiku TM, McShan AC, Evangelidis T, Nerli S, Carter L, Nivon LG, Davis A, Oberdorfer G, Tripsianes K, Sgourakis NG, Baker D Nat Struct Mol Biol. 2018 Nov;25(11):1028-1034. doi: 10.1038/s41594-018-0141-6., Epub 2018 Oct 29. PMID:30374087<ref>PMID:30374087</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 6e5c" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Synthetic construct sequences]]

[[Category: Baker, D]]

[[Category: Chidyausiku, T M]]

[[Category: Evangelidis, T]]

[[Category: Marcos, E]]

[[Category: McShan, A]]

[[Category: Nerli, S]]

[[Category: Sgourakis, N]]

[[Category: Tripsianes, K]]

[[Category: De novo protein]]