6vgb

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<StructureSection load='6vgb' size='340' side='right'caption='[[6vgb]]' scene=''>
<StructureSection load='6vgb' size='340' side='right'caption='[[6vgb]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VGB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VGB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6vgb]] 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=6VGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VGB FirstGlance]. <br>
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</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=6vgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vgb OCA], [http://pdbe.org/6vgb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vgb RCSB], [http://www.ebi.ac.uk/pdbsum/6vgb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vgb ProSAT]</span></td></tr>
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</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=6vgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vgb OCA], [https://pdbe.org/6vgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vgb RCSB], [https://www.ebi.ac.uk/pdbsum/6vgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vgb ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6vgb" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[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]]

Current revision

De novo designed Rossmann fold protein ROS2_36830

PDB ID 6vgb

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