NDLI: Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform

Content Provider	PubMed Central
Author	James, Thomas L. Liu, He Ulyanov, Nikolai B. Farr-jones, Shauna Zhang, Hong Donne, David G. Kaneko, Kiyotoshi Groth, Darlene Mehlhorn, Ingrid Prusiner, Stanley B. Cohen, Fred E.
Copyright Year	1997
Abstract	The scrapie prion protein (PrPSc) is the major, and possibly the only, component of the infectious prion; it is generated from the cellular isoform (PrPC) by a conformational change. N-terminal truncation of PrPSc by limited proteolysis produces a protein of ≈142 residues designated PrP 27–30, which retains infectivity. A recombinant protein (rPrP) corresponding to Syrian hamster PrP 27–30 was expressed in Escherichia coli and purified. After refolding rPrP into an α-helical form resembling PrPC, the structure was solved by multidimensional heteronuclear NMR, revealing many structural features of rPrP that were not found in two shorter PrP fragments studied previously. Extensive side-chain interactions for residues 113–125 characterize a hydrophobic cluster, which packs against an irregular β-sheet, whereas residues 90–112 exhibit little defined structure. Although identifiable secondary structure is largely lacking in the N terminus of rPrP, paradoxically this N terminus increases the amount of secondary structure in the remainder of rPrP. The surface of a long helix (residues 200–227) and a structured loop (residues 165–171) form a discontinuous epitope for binding of a protein that facilitates PrPSc formation. Polymorphic residues within this epitope seem to modulate susceptibility of sheep and humans to prion disease. Conformational heterogeneity of rPrP at the N terminus may be key to the transformation of PrPC into PrPSc, whereas the discontinuous epitope near the C terminus controls this transition.
Starting Page	10086
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	19
Volume Number	94
Language	English
Publisher	The National Academy of Sciences of the USA
Publisher Date	1997-09-16
Access Restriction	Open
Rights Holder	The National Academy of Sciences of the USA
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform.

Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform.

Three scrapie prion isolates exhibit different accumulation patterns of the prion protein scrapie isoform.

Disease-associated F198S Mutation Increases the Propensity of the Recombinant Prion Protein for Conformational Conversion to Scrapie-like Form

Unusual property of prion protein unfolding in neutral salt solution (2002)

Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform.

Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody

Recombinant scrapie-like prion protein of 106 amino acids is soluble

Amphotericin B inhibits the generation of the scrapie isoform of the prion protein in infected cultures (2000)

Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform

Similar Documents

Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform.

Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform.

Three scrapie prion isolates exhibit different accumulation patterns of the prion protein scrapie isoform.

Disease-associated F198S Mutation Increases the Propensity of the Recombinant Prion Protein for Conformational Conversion to Scrapie-like Form

Unusual property of prion protein unfolding in neutral salt solution (2002)

Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform.

Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody

Recombinant scrapie-like prion protein of 106 amino acids is soluble

Amphotericin B inhibits the generation of the scrapie isoform of the prion protein in infected cultures (2000)

Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform