View source for 2lta


==Solution NMR structure of De novo designed protein, rossmann 3x1 fold, Northeast Structural Genomics Consortium target OR157==
<StructureSection load='2lta' size='340' side='right'caption='[[2lta]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lta]] 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=2LTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LTA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lta OCA], [https://pdbe.org/2lta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lta RCSB], [https://www.ebi.ac.uk/pdbsum/2lta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lta ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Unlike random heteropolymers, natural proteins fold into unique ordered structures. Understanding how these are encoded in amino-acid sequences is complicated by energetically unfavourable non-ideal features--for example kinked alpha-helices, bulged beta-strands, strained loops and buried polar groups--that arise in proteins from evolutionary selection for biological function or from neutral drift. Here we describe an approach to designing ideal protein structures stabilized by completely consistent local and non-local interactions. The approach is based on a set of rules relating secondary structure patterns to protein tertiary motifs, which make possible the design of funnel-shaped protein folding energy landscapes leading into the target folded state. Guided by these rules, we designed sequences predicted to fold into ideal protein structures consisting of alpha-helices, beta-strands and minimal loops. Designs for five different topologies were found to be monomeric and very stable and to adopt structures in solution nearly identical to the computational models. These results illuminate how the folding funnels of natural proteins arise and provide the foundation for engineering a new generation of functional proteins free from natural evolution.

Principles for designing ideal protein structures.,Koga N, Tatsumi-Koga R, Liu G, Xiao R, Acton TB, Montelione GT, Baker D Nature. 2012 Nov 8;491(7423):222-7. doi: 10.1038/nature11600. PMID:23135467<ref>PMID:23135467</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: Acton TB]]
[[Category: Baker D]]
[[Category: Everett JK]]
[[Category: Hamilton K]]
[[Category: Koga N]]
[[Category: Koga R]]
[[Category: Kohan E]]
[[Category: Kornhaber G]]
[[Category: Liu G]]
[[Category: Montelione GT]]
[[Category: Pederson K]]
[[Category: Xiao R]]