1k5r: Difference between revisions
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==YAP65 WW domain S24-Amino-Ethylsulfanyl-Acetic Acid mutant== | ==YAP65 WW domain S24-Amino-Ethylsulfanyl-Acetic Acid mutant== | ||
<StructureSection load='1k5r' size='340' side='right'caption='[[1k5r | <StructureSection load='1k5r' size='340' side='right'caption='[[1k5r]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1k5r]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K5R FirstGlance]. <br> | <table><tr><td colspan='2'>[[1k5r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K5R FirstGlance]. <br> | ||
</td></tr><tr id=' | </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=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ESD:(2-AMINO-ETHYLSULFANYL)-ACETIC+ACID'>ESD</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1k5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k5r OCA], [https://pdbe.org/1k5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k5r RCSB], [https://www.ebi.ac.uk/pdbsum/1k5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k5r ProSAT]</span></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=1k5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k5r OCA], [https://pdbe.org/1k5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k5r RCSB], [https://www.ebi.ac.uk/pdbsum/1k5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k5r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/WBP1_HUMAN WBP1_HUMAN] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 33: | Line 33: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Daggett | [[Category: Daggett V]] | ||
[[Category: Ferguson | [[Category: Ferguson N]] | ||
[[Category: Fersht | [[Category: Fersht AR]] | ||
[[Category: Johnson | [[Category: Johnson CM]] | ||
[[Category: Oschkinat | [[Category: Oschkinat H]] | ||
[[Category: Pan | [[Category: Pan YP]] | ||
[[Category: Pires | [[Category: Pires JR]] | ||
[[Category: Schneider-Mergener | [[Category: Schneider-Mergener J]] | ||
[[Category: Toepert | [[Category: Toepert F]] | ||
[[Category: Volkmer-Engert | [[Category: Volkmer-Engert R]] | ||
Revision as of 10:55, 15 November 2023
YAP65 WW domain S24-Amino-Ethylsulfanyl-Acetic Acid mutantYAP65 WW domain S24-Amino-Ethylsulfanyl-Acetic Acid mutant
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedChemical synthesis allows the incorporation of nonnatural amino acids into proteins that may provide previously untried probes of their folding pathway and thermodynamic stability. We have used a flexible thioether linker as a loop mimetic in the human yes kinase-associated protein (YAP 65) WW domain, a three-stranded, 44-residue, beta-sheet protein. This linkage avoids problems of incorporating sequences that constrain loops to the extent that they significantly change the nature of the denatured state with concomitant effects on the folding kinetics. An NMR solution structure shows that the thioether linker had little effect on the global fold of the domain, although the loop is apparently more dynamic. The thioether variants are destabilized by up to 1.4 kcal/mol (1 cal = 4.18 J). Preliminary Phi-value analysis showed that the first loop is highly structured in the folding transition state, and the second loop is essentially unstructured. These data are consistent with results from simulated unfolding and detailed protein-engineering studies of structurally homologous WW domains. Previously, Phi-value analysis was limited to studying side-chain interactions. The linkers used here extend the protein engineering method directly to secondary-structure interactions. Using flexible loop mimetics to extend phi-value analysis to secondary structure interactions.,Ferguson N, Pires JR, Toepert F, Johnson CM, Pan YP, Volkmer-Engert R, Schneider-Mergener J, Daggett V, Oschkinat H, Fersht A Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):13008-13. Epub 2001 Oct 30. PMID:11687614[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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