View source for 6llq


==Solution NMR structure of de novo Rossmann2x2 fold with most of the core mutated to valine, R2x2_VAL88==
<StructureSection load='6llq' size='340' side='right'caption='[[6llq]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6llq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LLQ FirstGlance]. <br>
</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=6llq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6llq OCA], [https://pdbe.org/6llq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6llq RCSB], [https://www.ebi.ac.uk/pdbsum/6llq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6llq ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Protein design provides a stringent test for our understanding of protein folding. We previously described principles for designing ideal protein structures stabilized by consistent local and nonlocal interactions, based on a set of rules relating local backbone structures to tertiary packing motifs. The principles have made possible the design of protein structures having various topologies with high thermal stability. Whereas nonlocal interactions such as tight hydrophobic core packing have traditionally been considered to be crucial for protein folding and stability, the rules proposed by our previous studies suggest the importance of local backbone structures to protein folding. In this study, we investigated the robustness of folding of de novo designed proteins to the reduction of the hydrophobic core, by extensive mutation of large hydrophobic residues (Leu, Ile) to smaller ones (Val) for one of the designs. Surprisingly, even after 10 Leu and Ile residues were mutated to Val, this mutant with the core mostly filled with Val was found to not be in a molten globule state and fold into the same backbone structure as the original design, with high stability. These results indicate the importance of local backbone structures to the folding ability and high thermal stability of designed proteins and suggest a method for engineering thermally stabilized natural proteins.

Robust folding of a de novo designed ideal protein even with most of the core mutated to valine.,Koga R, Yamamoto M, Kosugi T, Kobayashi N, Sugiki T, Fujiwara T, Koga N Proc Natl Acad Sci U S A. 2020 Dec 8;117(49):31149-31156. doi:, 10.1073/pnas.2002120117. Epub 2020 Nov 23. PMID:33229587<ref>PMID:33229587</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 6llq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Unidentified]]
[[Category: Fujiwara T]]
[[Category: Kobayashi N]]
[[Category: Koga N]]
[[Category: Koga R]]
[[Category: Kosugi T]]
[[Category: Sugiki T]]
[[Category: Yamamoto M]]