6vg7: Difference between revisions

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<StructureSection load='6vg7' size='340' side='right'caption='[[6vg7]]' scene=''>
<StructureSection load='6vg7' size='340' side='right'caption='[[6vg7]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VG7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VG7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6vg7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VG7 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vg7 OCA], [http://pdbe.org/6vg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vg7 RCSB], [http://www.ebi.ac.uk/pdbsum/6vg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vg7 ProSAT]</span></td></tr>
</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=6vg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vg7 OCA], [https://pdbe.org/6vg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vg7 RCSB], [https://www.ebi.ac.uk/pdbsum/6vg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vg7 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Naturally occurring proteins vary the precise geometries of structural elements to create distinct shapes optimal for function. We present a computational design method, loop-helix-loop unit combinatorial sampling (LUCS), that mimics nature's ability to create families of proteins with the same overall fold but precisely tunable geometries. Through near-exhaustive sampling of loop-helix-loop elements, LUCS generates highly diverse geometries encompassing those found in nature but also surpassing known structure space. Biophysical characterization showed that 17 (38%) of 45 tested LUCS designs encompassing two different structural topologies were well folded, including 16 with designed non-native geometries. Four experimentally solved structures closely matched the designs. LUCS greatly expands the designable structure space and offers a new paradigm for designing proteins with tunable geometries that may be customizable for novel functions.
Expanding the space of protein geometries by computational design of de novo fold families.,Pan X, Thompson MC, Zhang Y, Liu L, Fraser JS, Kelly MJS, Kortemme T Science. 2020 Aug 28;369(6507):1132-1136. doi: 10.1126/science.abc0881. PMID:32855341<ref>PMID:32855341</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6vg7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Kelly M]]
[[Category: Kelly M]]
[[Category: Kortemme T]]
[[Category: Kortemme T]]
[[Category: Pan X]]
[[Category: Pan X]]
[[Category: Zhang Y]]
[[Category: Zhang Y]]

Latest revision as of 11:05, 14 June 2023

De novo designed Rossmann fold protein ROS2_49223

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