Unraveling the Cu2+Binding Sites in the C-Terminal Domain of the Murine Prion Protein:  A Pulse EPR and ENDOR Study†

2001 ◽  
Vol 105 (8) ◽  
pp. 1631-1639 ◽  
Author(s):  
Sabine Van Doorslaer ◽  
Grazia M. Cereghetti ◽  
Rudi Glockshuber ◽  
Arthur Schweiger
Keyword(s):  
Prion Protein ◽  
Binding Sites ◽  
Protein A ◽  
Terminal Domain ◽  
Pulse Epr

Copper binding sites in the C‐terminal domain of mouse prion protein: A hybrid (QM/MM) molecular dynamics study

2008 ◽  
Vol 70 (3) ◽  
pp. 1084-1098 ◽  
Author(s):  
Maria Carola Colombo ◽  
Joost VandeVondele ◽  
Sabine Van Doorslaer ◽  
Alessandro Laio ◽  
Leonardo Guidoni ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Prion Protein ◽  
Binding Sites ◽  
Protein A ◽  
Copper Binding ◽  
Terminal Domain ◽  
Copper Binding Sites

scholarly journals Identification of the Cu2+Binding Sites in the N-Terminal Domain of the Prion Protein by EPR and CD Spectroscopy†

Biochemistry ◽  
2000 ◽  
Vol 39 (45) ◽  
pp. 13760-13771 ◽  
Author(s):  
Eliah Aronoff-Spencer ◽  
Colin S. Burns ◽  
Nikolai I. Avdievich ◽  
Gary J. Gerfen ◽  
Jack Peisach ◽  
...  
Keyword(s):  
Prion Protein ◽  
Binding Sites ◽  
Cd Spectroscopy ◽  
Terminal Domain

scholarly journals Biological Functions of the Intrinsically Disordered N-Terminal Domain of the Prion Protein: A Possible Role of Liquid–Liquid Phase Separation

Biomolecules ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 1201
Author(s):  
Stella A. Polido ◽  
Janine Kamps ◽  
Jörg Tatzelt
Keyword(s):  
Prion Protein ◽  
Tertiary Structure ◽  
Polypeptide Chain ◽  
Protein A ◽  
Interacting Proteins ◽  
Intrinsically Disordered ◽  
Terminal Domain ◽  
Protein Classes ◽  
Liquid Liquid Phase Separation

The mammalian prion protein (PrPC) is composed of a large intrinsically disordered N-terminal and a structured C-terminal domain, containing three alpha-helical regions and a short, two-stranded beta-sheet. Traditionally, the activity of a protein was linked to the ability of the polypeptide chain to adopt a stable secondary/tertiary structure. This concept has been extended when it became evident that intrinsically disordered domains (IDDs) can participate in a broad range of defined physiological activities and play a major functional role in several protein classes including transcription factors, scaffold proteins, and signaling molecules. This ability of IDDs to engage in a variety of supramolecular complexes may explain the large number of PrPC-interacting proteins described. Here, we summarize diverse physiological and pathophysiological activities that have been described for the unstructured N-terminal domain of PrPC. In particular, we focus on subdomains that have been conserved in evolution.

scholarly journals Determinants of carboxyl-terminal domain translocation during prion protein biogenesis

1994 ◽  
Vol 269 (24) ◽  
pp. 16810-16820
Author(s):  
K.A. De Fea ◽  
D.H. Nakahara ◽  
M.C. Calayag ◽  
C.S. Yost ◽  
L.F. Mirels ◽  
...  
Keyword(s):  
Prion Protein ◽  
Terminal Domain ◽  
Carboxyl Terminal Domain ◽  
Protein Biogenesis ◽  
Carboxyl Terminal

scholarly journals Interaction of calcium ions and salivary acidic proline-rich proteins with hydroxyapatite. A possible aspect of inhibition of hydroxyapatite formation

1983 ◽  
Vol 213 (1) ◽  
pp. 11-20 ◽  
Author(s):  
A Bennick ◽  
D Kells ◽  
G Madapallimattam
Keyword(s):  
Crystal Growth ◽  
Calcium Ions ◽  
Binding Sites ◽  
Protein C ◽  
Tryptic Peptide ◽  
Protein A ◽  
Additional Amount ◽  
The Relationship ◽  
Surrounding Liquid ◽  
Hydroxyapatite Formation

The relationship between Ca2+- and hydroxyapatite-binding sites in salivary acidic proline-rich phosphoproteins A and C was investigated. Coating of hydroxyapatite with protein before adsorption had no effect on Ca2+ binding to the mineral, but simultaneous adsorption of Ca+ and protein to hydroxyapatite caused additional Ca2+ binding to the solid. The additional amount of Ca2+ adsorbed, measured in mol of Ca2+/mol of protein adsorbed to hydroxyapatite, was approx. 2 for protein C, 4 for protein A, 9 for the N-terminal tryptic peptide and 2 for dephosphorylated protein A. It is suggested that the ability of the proteins to inhibit hydroxyapatite formation is related to the binding of the proteins to crystal growth sites on the mineral, which prevents access of Ca2+ from the surrounding liquid.

The complex-formation behaviour of His residues in the fifth Cu2+ binding site of human prion protein: a close look

2009 ◽  
Vol 33 (11) ◽  
pp. 2300 ◽  
Author(s):  
Maurizio Remelli ◽  
Daniela Valensin ◽  
Dimitri Bacco ◽  
Ewa Gralka ◽  
Remo Guerrini ◽  
...  
Keyword(s):  
Complex Formation ◽  
Binding Site ◽  
Prion Protein ◽  
Protein A ◽  
Human Prion Protein

scholarly journals Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus

2003 ◽  
Vol 31 (3) ◽  
pp. 716-718 ◽  
Author(s):  
N.G. Housden ◽  
S. Harrison ◽  
S.E. Roberts ◽  
J.A. Beckingham ◽  
M. Graille ◽  
...  
Keyword(s):  
Binding Sites ◽  
Protein A ◽  
Cell Wall Protein ◽  
Protein G ◽  
Protein L ◽  
Heavy Chains ◽  
Binding Domains ◽  
Peptostreptococcus Magnus ◽  
Immunoglobulin Binding

Protein L is a multidomain cell-wall protein isolated from Peptostreptococcus magnus. It belongs to a group of proteins that contain repeated domains that are able to bind to Igs without stimulating an immune response, the most characterized of this group being Protein A (Staphylococcus aureus) and Protein G (Streptococcus). Both of these proteins bind predominantly to the interface of CH2-CH3 heavy chains, while Protein L binds exclusively to the VL domain of the κ-chain. The function of these proteins in vivo is not clear but it is thought that they enable the bacteria to evade the host's immune system. Two binding sites for κ-chain on a single Ig-binding domain from Protein L have recently been reported and we give evidence that one site has a 25–55-fold higher affinity for κ-chain than the second site.

scholarly journals Rapid and Low-Input Profiling of Histone Marks in Plants Using Nucleus CUT&Tag

2021 ◽  
Vol 12 ◽  
Author(s):  
Weizhi Ouyang ◽  
Xiwen Zhang ◽  
Yong Peng ◽  
Qing Zhang ◽  
Zhilin Cao ◽  
...  
Keyword(s):  
Histone Modifications ◽  
Chromatin Immunoprecipitation ◽  
Binding Sites ◽  
Protein A ◽  
Transcriptional Factor ◽  
Experimental Procedure ◽  
Histone Marks ◽  
Genome Wide ◽  
Efficient Alternative ◽  
Tn5 Transposase

Characterizing genome-wide histone posttranscriptional modifications and transcriptional factor occupancy is crucial for deciphering their biological functions. Chromatin immunoprecipitation followed by sequencing (ChIP-seq) is a powerful method for genome-wide profiling of histone modifications and transcriptional factor-binding sites. However, the current ChIP-seq experimental procedure in plants requires significant material and several days for completion. CUT&Tag is an alternative method of ChIP-seq for low-sample and single-cell epigenomic profiling using protein A-Tn5 transposase fusion proteins (PAT). In this study, we developed a nucleus CUT&Tag (nCUT&Tag) protocol based on the live-cell CUT&Tag technology. Our results indicate that nCUT&Tag could be used for histone modifications profiling in both monocot rice and dicot rapeseed using crosslinked or fresh tissues. In addition, both active and repressive histone marks such as H3K4me3 and H3K9me2 can be identified using our nCUT&Tag. More importantly, all the steps in nCUT&Tag can be finished in only 1 day, and the assay can be performed with as little as 0.01 g of plant tissue as starting materials. Therefore, our results demonstrate that nCUT&Tag is an efficient alternative strategy for plant epigenomic studies.

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