5kpe: Difference between revisions
No edit summary |
No edit summary |
||
(4 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
==Solution NMR Structure of Denovo Beta Sheet Design Protein, Northeast Structural Genomics Consortium (NESG) Target OR664== | ==Solution NMR Structure of Denovo Beta Sheet Design Protein, Northeast Structural Genomics Consortium (NESG) Target OR664== | ||
<StructureSection load='5kpe' size='340' side='right' caption='[[5kpe | <StructureSection load='5kpe' size='340' side='right'caption='[[5kpe]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5kpe]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KPE OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5kpe]] 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=5KPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KPE FirstGlance]. <br> | ||
</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=5kpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kpe OCA], [https://pdbe.org/5kpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kpe RCSB], [https://www.ebi.ac.uk/pdbsum/5kpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kpe ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Active sites and ligand-binding cavities in native proteins are often formed by curved beta sheets, and the ability to control beta-sheet curvature would allow design of binding proteins with cavities customized to specific ligands. Toward this end, we investigated the mechanisms controlling beta-sheet curvature by studying the geometry of beta sheets in naturally occurring protein structures and folding simulations. The principles emerging from this analysis were used to design, de novo, a series of proteins with curved beta sheets topped with alpha helices. Nuclear magnetic resonance and crystal structures of the designs closely match the computational models, showing that beta-sheet curvature can be controlled with atomic-level accuracy. Our approach enables the design of proteins with cavities and provides a route to custom design ligand-binding and catalytic sites. | |||
Principles for designing proteins with cavities formed by curved beta sheets.,Marcos E, Basanta B, Chidyausiku TM, Tang Y, Oberdorfer G, Liu G, Swapna GV, Guan R, Silva DA, Dou J, Pereira JH, Xiao R, Sankaran B, Zwart PH, Montelione GT, Baker D Science. 2017 Jan 13;355(6321):201-206. doi: 10.1126/science.aah7389. PMID:28082595<ref>PMID:28082595</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5kpe" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Baker D]] | ||
[[Category: | [[Category: Liu G]] | ||
[[Category: | [[Category: Montelione GT]] | ||
[[Category: | [[Category: Tang Y]] |
Latest revision as of 13:13, 14 June 2023
Solution NMR Structure of Denovo Beta Sheet Design Protein, Northeast Structural Genomics Consortium (NESG) Target OR664Solution NMR Structure of Denovo Beta Sheet Design Protein, Northeast Structural Genomics Consortium (NESG) Target OR664
Structural highlights
Publication Abstract from PubMedActive sites and ligand-binding cavities in native proteins are often formed by curved beta sheets, and the ability to control beta-sheet curvature would allow design of binding proteins with cavities customized to specific ligands. Toward this end, we investigated the mechanisms controlling beta-sheet curvature by studying the geometry of beta sheets in naturally occurring protein structures and folding simulations. The principles emerging from this analysis were used to design, de novo, a series of proteins with curved beta sheets topped with alpha helices. Nuclear magnetic resonance and crystal structures of the designs closely match the computational models, showing that beta-sheet curvature can be controlled with atomic-level accuracy. Our approach enables the design of proteins with cavities and provides a route to custom design ligand-binding and catalytic sites. Principles for designing proteins with cavities formed by curved beta sheets.,Marcos E, Basanta B, Chidyausiku TM, Tang Y, Oberdorfer G, Liu G, Swapna GV, Guan R, Silva DA, Dou J, Pereira JH, Xiao R, Sankaran B, Zwart PH, Montelione GT, Baker D Science. 2017 Jan 13;355(6321):201-206. doi: 10.1126/science.aah7389. PMID:28082595[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|