Solution structure of an active mutant of maize ribosome-inactivating protein (MOD) and its interaction with the ribosomal stalk protein P2
about
Structures of the ribosome-inactivating protein from barley seeds reveal a unique activation mechanismStructures and Ribosomal Interaction of Ribosome-Inactivating ProteinsPokeweed antiviral protein: its cytotoxicity mechanism and applications in plant disease resistanceFunctional divergence between the two P1-P2 stalk dimers on the ribosome in their interaction with ricin A chainHuman ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with a prominent role for P1 C-terminus.Interaction of ricin and Shiga toxins with ribosomesCharged and hydrophobic surfaces on the a chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteinsPentameric organization of the ribosomal stalk accelerates recruitment of ricin a chain to the ribosome for depurination.Maize ribosome-inactivating protein uses Lys158-lys161 to interact with ribosomal protein P2 and the strength of interaction is correlated to the biological activities.Shiga toxin 1 is more dependent on the P proteins of the ribosomal stalk for depurination activity than Shiga toxin 2Arginine residues on the opposite side of the active site stimulate the catalysis of ribosome depurination by ricin A chain by interacting with the P-protein stalkCrystal Structure of Ribosome-Inactivating Protein Ricin A Chain in Complex with the C-Terminal Peptide of the Ribosomal Stalk Protein P2.Ricin uses arginine 235 as an anchor residue to bind to P-proteins of the ribosomal stalk.Extensive Evolution of Cereal Ribosome-Inactivating Proteins Translates into Unique Structural Features, Activation Mechanisms, and Physiological RolesA switch-on mechanism to activate maize ribosome-inactivating protein for targeting HIV-infected cells.Improvement of the Pharmacological Properties of Maize RIP by Cysteine-Specific PEGylation.The acidic ribosomal protein P2 from Euplotes octocarinatus is phosphorylated at its N-terminal domain.Structural and Functional Investigation and Pharmacological Mechanism of Trichosanthin, a Type 1 Ribosome-Inactivating Protein
P2860
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P2860
Solution structure of an active mutant of maize ribosome-inactivating protein (MOD) and its interaction with the ribosomal stalk protein P2
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Solution structure of an activ ...... the ribosomal stalk protein P2
@ast
Solution structure of an activ ...... the ribosomal stalk protein P2
@en
Solution structure of an activ ...... the ribosomal stalk protein P2
@nl
type
label
Solution structure of an activ ...... the ribosomal stalk protein P2
@ast
Solution structure of an activ ...... the ribosomal stalk protein P2
@en
Solution structure of an activ ...... the ribosomal stalk protein P2
@nl
prefLabel
Solution structure of an activ ...... the ribosomal stalk protein P2
@ast
Solution structure of an activ ...... the ribosomal stalk protein P2
@en
Solution structure of an activ ...... the ribosomal stalk protein P2
@nl
P2093
P3181
P1476
Solution structure of an activ ...... the ribosomal stalk protein P2
@en
P2093
Amanda Nga-Sze Mak
Kong Hung Sze
Pang-Chui Shaw
Yinhua Yang
P304
P3181
P356
10.1016/J.JMB.2009.10.051
P407
P577
2010-02-05T00:00:00Z