5uce: Difference between revisions
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==Solution NMR structure of the major species of DANCER-2, a dynamic and natively folded pentamutant of the B1 domain of streptococcal protein G (GB1)== | |||
<StructureSection load='5uce' size='340' side='right'caption='[[5uce]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5uce]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._GX7805 Streptococcus sp. GX7805]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UCE 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=5uce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uce OCA], [https://pdbe.org/5uce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uce RCSB], [https://www.ebi.ac.uk/pdbsum/5uce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uce ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SPG2_STRSG SPG2_STRSG] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Proteins are intrinsically dynamic molecules that can exchange between multiple conformational states, enabling them to carry out complex molecular processes with extreme precision and efficiency. Attempts to design novel proteins with tailored functions have mostly failed to yield efficiencies matching those found in nature because standard methods do not allow the design of exchange between necessary conformational states on a functionally relevant timescale. Here we developed a broadly applicable computational method to engineer protein dynamics that we term meta-multistate design. We used this methodology to design spontaneous exchange between two novel conformations introduced into the global fold of Streptococcal protein G domain beta1. The designed proteins, named DANCERs, for dynamic and native conformational exchangers, are stably folded and switch between predicted conformational states on the millisecond timescale. The successful introduction of defined dynamics on functional timescales opens the door to new applications requiring a protein to spontaneously access multiple conformational states. | |||
Rational design of proteins that exchange on functional timescales.,Davey JA, Damry AM, Goto NK, Chica RA Nat Chem Biol. 2017 Oct 23. doi: 10.1038/nchembio.2503. PMID:29058725<ref>PMID:29058725</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5uce" style="background-color:#fffaf0;"></div> | ||
[[Category: Chica | |||
[[Category: | ==See Also== | ||
[[Category: Davey | *[[Protein G|Protein G]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus sp. GX7805]] | |||
[[Category: Chica RA]] | |||
[[Category: Damry AM]] | |||
[[Category: Davey JA]] | |||
[[Category: Goto NK]] | |||
Latest revision as of 13:25, 14 June 2023
Solution NMR structure of the major species of DANCER-2, a dynamic and natively folded pentamutant of the B1 domain of streptococcal protein G (GB1)Solution NMR structure of the major species of DANCER-2, a dynamic and natively folded pentamutant of the B1 domain of streptococcal protein G (GB1)
Structural highlights
FunctionPublication Abstract from PubMedProteins are intrinsically dynamic molecules that can exchange between multiple conformational states, enabling them to carry out complex molecular processes with extreme precision and efficiency. Attempts to design novel proteins with tailored functions have mostly failed to yield efficiencies matching those found in nature because standard methods do not allow the design of exchange between necessary conformational states on a functionally relevant timescale. Here we developed a broadly applicable computational method to engineer protein dynamics that we term meta-multistate design. We used this methodology to design spontaneous exchange between two novel conformations introduced into the global fold of Streptococcal protein G domain beta1. The designed proteins, named DANCERs, for dynamic and native conformational exchangers, are stably folded and switch between predicted conformational states on the millisecond timescale. The successful introduction of defined dynamics on functional timescales opens the door to new applications requiring a protein to spontaneously access multiple conformational states. Rational design of proteins that exchange on functional timescales.,Davey JA, Damry AM, Goto NK, Chica RA Nat Chem Biol. 2017 Oct 23. doi: 10.1038/nchembio.2503. PMID:29058725[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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