ArticleJournal of molecular biology2010
Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 54 citations in OpenAlex.
- A tetracationic porphyrin with dual anti-prion activity.iScience · 2023Article
- Prion Protein Octarepeat Domain Forms Transient β-Sheet Structures upon Residue-Specific Binding to Cu(II) and Zn(II) Ions.Biochemistry · 2023Article
- Pentosan polysulfate induces low-level persistent prion infection keeping measurable seeding activity without PrP-res detection in Fukuoka-1 infected cell cultures.Scientific reports · 2022Article
- Unfolded and intermediate states of PrP play a key role in the mechanism of action of an antiprion chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Prion Protein at the Leading Edge: Its Role in Cell Motility.International journal of molecular sciences · 2020Review
- ODiNPred: comprehensive prediction of protein order and disorder.Scientific reports · 2020Article
- N-Terminal Regions of Prion Protein: Functions and Roles in Prion Diseases.International journal of molecular sciences · 2020Review
- The N-Terminal Polybasic Region of Prion Protein Is Crucial in Prion Pathogenesis Independently of the Octapeptide Repeat Region.Molecular neurobiology · 2020Article
- Melanin or a Melanin-Like Substance Interacts with the N-Terminal Portion of Prion Protein and Inhibits Abnormal Prion Protein Formation in Prion-Infected Cells.Journal of virology · 2017Article
- Physiological Functions of the Cellular Prion Protein.Frontiers in molecular biosciences · 2017Review
- Heparan Sulfate and Heparin Promote Faithful Prion Replication in Vitro by Binding to Normal and Abnormal Prion Proteins in Protein Misfolding Cyclic Amplification.The Journal of biological chemistry · 2016Article
- The N Terminus of the Prion Protein Mediates Functional Interactions with the Neuronal Cell Adhesion Molecule (NCAM) Fibronectin Domain.The Journal of biological chemistry · 2016Article
- Expression of Tyrosine Hydroxylase is Negatively Regulated Via Prion Protein.Neurochemical research · 2016Article
- Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein.Scientific reports · 2015Article
- Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation.EMBO molecular medicine · 2015Article
- Combined EXAFS and DFT structure calculations provide structural insights into the 1:1 multi-histidine complexes of Cu(II) , Cu(I) , and Zn(II) with the tandem octarepeats of the mammalian prion protein.Chemistry (Weinheim an der Bergstrasse, Germany) · 2014Article
- The crystal structure of an octapeptide repeat of the prion protein in complex with a Fab fragment of the POM2 antibody.Protein science : a publication of the Protein Society · 2013Article
- Anti-prion activity of an RNA aptamer and its structural basis.Nucleic acids research · 2013Article
- The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc).The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Allosteric function and dysfunction of the prion protein.Cellular and molecular life sciences : CMLS · 2012Review
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The intrinsically disordered amino-proximal domain of hamster prion protein (PrP) contains four copies of a highly conserved octapeptide sequence, PHGGGWGQ, that is flanked by two polycationic residue clusters. This N-terminal domain mediates the binding of sulfated glycans, which can profoundly influence the conversion of PrP to pathological forms and the progression of prion disease. To investigate the structural consequences of sulfated glycan binding, we performed multidimensional heteronuclear ((1)H, (13)C, (15)N) NMR (nuclear magnetic resonance), circular dichroism (CD), and fluorescence studies on hamster PrP residues 23-106 (PrP 23-106) and fragments thereof when bound to pentosan polysulfate (PPS). While the majority of PrP 23-106 remain disordered upon PPS binding, the octarepeat region adopts a repeating loop-turn structure that we have determined by NMR. The beta-like turns within the repeats are corroborated by CD data demonstrating that these turns are also present, although less pronounced, without PPS. Binding to PPS exposes a hydrophobic surface composed of aligned tryptophan side chains, the spacing and orientation of which are consistent with a self-association or ligand binding site. The unique tryptophan motif was probed by intrinsic tryptophan fluorescence, which displayed enhanced fluorescence of PrP 23-106 when bound to PPS, consistent with the alignment of tryptophan side chains. Chemical-shift mapping identified binding sites on PrP 23-106 for PPS, which include the octarepeat histidine and an N-terminal basic cluster previously linked to sulfated glycan binding. These data may in part explain how sulfated glycans modulate PrP conformational conversions and oligomerizations.
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