1h0l: Difference between revisions
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==HUMAN PRION PROTEIN 121-230 M166C/E221C== | ==HUMAN PRION PROTEIN 121-230 M166C/E221C== | ||
<StructureSection load='1h0l' size='340' side='right' caption='[[1h0l]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1h0l' size='340' side='right'caption='[[1h0l]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1h0l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H0L FirstGlance]. <br> | <table><tr><td colspan='2'>[[1h0l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H0L FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Doppel|Doppel]] | *[[Doppel|Doppel]] | ||
*[[Prion|Prion]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Guntert, P]] | [[Category: Guntert, P]] | ||
[[Category: Wuthrich, K]] | [[Category: Wuthrich, K]] | ||
Revision as of 12:08, 23 October 2019
HUMAN PRION PROTEIN 121-230 M166C/E221CHUMAN PRION PROTEIN 121-230 M166C/E221C
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe nuclear magnetic resonance structure of the globular domain with residues 121-230 of a variant human prion protein with two disulfide bonds, hPrP(M166C/E221C), shows the same global fold as wild-type hPrP(121-230). It contains three alpha-helices of residues 144-154, 173-194 and 200-228, an anti-parallel beta-sheet of residues 128-131 and 161-164, and the disulfides Cys166-Cys221 and Cys179-Cys214. The engineered extra disulfide bond in the presumed "protein X"-binding site is accommodated with slight, strictly localized conformational changes. High compatibility of hPrP with insertion of a second disulfide bridge in the protein X epitope was further substantiated by model calculations with additional variant structures. The ease with which the hPrP structure can accommodate a variety of locations for a second disulfide bond within the presumed protein X-binding epitope suggests a functional role for the extensive perturbation by a natural second disulfide bond of the corresponding region in the human doppel protein. NMR structure of a variant human prion protein with two disulfide bridges.,Zahn R, Guntert P, von Schroetter C, Wuthrich K J Mol Biol. 2003 Feb 7;326(1):225-34. PMID:12547204[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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