1k5r: Difference between revisions

Revision as of 09:49, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1k5r.png

Template:STRUCTURE 1k5r

YAP65 WW domain S24-Amino-Ethylsulfanyl-Acetic Acid mutantYAP65 WW domain S24-Amino-Ethylsulfanyl-Acetic Acid mutant

Template:ABSTRACT PUBMED 11687614

About this StructureAbout this Structure

1K5R is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Wed Jul 2 09:49:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1k5r.gif|left|200px]]
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 {{STRUCTURE_1k5r|  PDB=1k5r  |  SCENE=  }}
-'''YAP65 WW domain S24-Amino-Ethylsulfanyl-Acetic Acid mutant'''
+===YAP65 WW domain S24-Amino-Ethylsulfanyl-Acetic Acid mutant===
-==Overview==
+<!--
-Chemical 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11687614}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11687614 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11687614}}
 ==About this Structure==
-K5R is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K5R OCA].
+K5R is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K5R OCA].
 ==Reference==
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 [[Category: Ww domain]]
 [[Category: Yap65]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:20:44 2008''
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