scholarly journals Role of Asn2 and Glu7 residues in the oxidative folding and on the conformation of theN-terminal loop of apamin

Biopolymers ◽  
2007 ◽  
Vol 86 (5-6) ◽  
pp. 447-462 ◽  
Author(s):  
Dung Le-Nguyen ◽  
Laurent Chiche ◽  
François Hoh ◽  
Marie France Martin-Eauclaire ◽  
Christian Dumas ◽  
...  
Keyword(s):  
Oxidative Folding ◽  
Terminal Loop

Role of the 14-3-3 C-terminal loop in ligand interaction

2002 ◽  
Vol 49 (3) ◽  
pp. 321-325 ◽  
Author(s):  
Amy B. Truong ◽  
Shane C. Masters ◽  
Hongzhu Yang ◽  
Haian Fu
Keyword(s):  
Ligand Interaction ◽  
Terminal Loop

scholarly journals A Lys49 PhospholipaseA2, Isolated fromBothrops asperSnake Venom, Induces Lipid Droplet Formation in Macrophages Which Depends on Distinct Signaling Pathways and the C-Terminal Region

2013 ◽  
Vol 2013 ◽  
pp. 1-14 ◽  
Author(s):  
Karina Cristina Giannotti ◽  
Elbio Leiguez ◽  
Vanessa Moreira ◽  
Neide Galvão Nascimento ◽  
Bruno Lomonte ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Protein Kinases ◽  
Inflammatory Responses ◽  
Critical Role ◽  
Terminal Sequence ◽  
Pharmacological Interventions ◽  
C Terminus ◽  
Inflammatory Mechanism ◽  
Terminal Loop

MT-II, a Lys49PLA2homologue devoid of catalytic activity fromB. aspervenom, stimulates inflammatory events in macrophages. We investigated the ability of MT-II to induce formation of lipid droplets (LDs), key elements of inflammatory responses, in isolated macrophages and participation of protein kinases and intracellular PLA2s in this effect. Influence of MT-II on PLIN2 recruitment and expression was assessed, and the effects of some synthetic peptides on LD formation were further evaluated. At noncytotoxic concentrations, MT-II directly activated macrophages to form LDs. This effect was reproduced by a synthetic peptide corresponding to the C-terminal sequence 115–129 of MT-II, evidencing the critical role of C-terminus for MT-II-induced effect. Moreover, MT-II induced expression and recruitment of PLIN2. Pharmacological interventions with specific inhibitors showed that PKC, PI3K, ERK1/2, and iPLA2, but notP38MAPKor cPLA2, signaling pathways are involved in LD formation induced by MT-II. This sPLA2homologue also induced synthesis of PGE2that colocalized to LDs. In conclusion, MT-II is able to induce formation of LDs committed to PGE2formation in a process dependent on C-terminal loop engagement and regulated by distinct protein kinases and iPLA2. LDs may constitute an important inflammatory mechanism triggered by MT-II in macrophages.

Role of an N-Terminal Loop in the Secondary Structural Change of Photoactive Yellow Protein†

Biochemistry ◽  
2003 ◽  
Vol 42 (47) ◽  
pp. 13893-13900 ◽  
Author(s):  
Miki Harigai ◽  
Yasushi Imamoto ◽  
Hironari Kamikubo ◽  
Yoichi Yamazaki ◽  
Mikio Kataoka
Keyword(s):  
Structural Change ◽  
Photoactive Yellow Protein ◽  
Terminal Loop ◽  
Secondary Structural Change

scholarly journals The role of the N-terminal loop in the function of the colicin E7 nuclease domain

2013 ◽  
Vol 18 (3) ◽  
pp. 309-321 ◽  
Author(s):  
Anikó Czene ◽  
Eszter Németh ◽  
István G. Zóka ◽  
Noémi I. Jakab-Simon ◽  
Tamás Körtvélyesi ◽  
...  
Keyword(s):  
Nuclease Domain ◽  
Colicin E7 ◽  
Terminal Loop

scholarly journals Ultra-Rapid Glutathionylation of Ribonuclease: Is this the Real Incipit of its Oxidative Folding?

2019 ◽  
Vol 20 (21) ◽  
pp. 5440 ◽  
Author(s):  
Bocedi ◽  
Cattani ◽  
Gambardella ◽  
Ticconi ◽  
Cozzolino ◽  
...  
Keyword(s):  
Molten Globule ◽  
Ribonuclease A ◽  
Early Step ◽  
Oxidative Folding ◽  
Nitrobenzoic Acid ◽  
Pka Value ◽  
High Concentrations ◽  
Protein Disulfide ◽  
Shed Light

Many details of oxidative folding of proteins remain obscure, in particular, the role of oxidized glutathione (GSSG). This study reveals some unknown aspects. When a reduced ribonuclease A refolds in the presence of GSSG, most of its eight cysteines accomplish a very fast glutathionylation. In particular, one single cysteine, identified as Cys95 by mass spectrometry, displays 3600 times higher reactivity when compared with an unperturbed protein cysteine. Furthermore, the other five cysteines show 40–50 times higher reactivity toward GSSG. This phenomenon is partially due to a low pKa value of most of these cysteines (average pKa = 7.9), but the occurrence of a reversible GSSG-ribonuclease complex (KD = 0.12 mM) is reasonably responsible for the extraordinary hyper-reactivity of Cys95. Neither hyper-reactivity nor some protein-disulfide complexes have been found by reacting a reduced ribonuclease with other natural disulfides i.e., cystine, cystamine, and homocystine. Hyper-reactivity of all cysteines was observed toward 5,5’-dithiobis-(2-nitrobenzoic acid). Given that GSSG is present in high concentrations in the endoplasmic reticulum, this property may shed light on the early step of its oxidative folding. The ultra-rapid glutathionylation of cysteines, only devoted to form disulfides, is a novel property of the molten globule status of the ribonuclease.

Role of the [65−72] Disulfide Bond in Oxidative Folding of Bovine Pancreatic Ribonuclease A†

Biochemistry ◽  
2003 ◽  
Vol 42 (39) ◽  
pp. 11514-11519 ◽  
Author(s):  
Hang-Cheol Shin ◽  
Mahesh Narayan ◽  
Myeong-Cheol Song ◽  
Harold A. Scheraga
Keyword(s):  
Disulfide Bond ◽  
Ribonuclease A ◽  
Oxidative Folding ◽  
Pancreatic Ribonuclease ◽  
Pancreatic Ribonuclease A

scholarly journals The N-Terminal Helix-Turn-Helix Motif of Transcription Factors MarA and Rob Drives DNA Recognition

2020 ◽  
Author(s):  
Marina Corbella ◽  
Qinghua Liao ◽  
Peter M. Kasson ◽  
Shina Caroline Lynn Kamerlin
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Dna Sequences ◽  
Dynamical Behavior ◽  
Dna Recognition ◽  
Tight Binding ◽  
Binding Mode ◽  
Efficient Design ◽  
Terminal Loop

<div> <div> <div> <p>DNA-binding proteins play an important role in gene regulation and cellular function. The transcription factors MarA and Rob are two homologous members of the AraC/XylS family that regulate multidrug resistance. They share a common DNA-binding domain, and Rob possesses an additional C-terminal domain that permits binding of low-molecular weight effectors. Both proteins possess two helix-turn- helix (HTH) motifs capable of binding DNA; however, while MarA interacts with its promoter through both HTH-motifs, prior studies indicate that Rob binding to DNA via a single HTH-motif is sufficient for tight binding. In the present work, we perform microsecond time scale all-atom simulations of the binding of both transcription factors to different DNA sequences to understand the determinants of DNA recognition and binding. Our simulations characterize sequence-specific changes in the dynamical behavior upon DNA binding, showcasing the role of Arg40 of the N-terminal HTH-motif in allowing for specific tight binding. Finally, our simulations explain how an acidic C-terminal loop of Rob can control DNA binding mode. In doing so, we provide detailed molecular insight into DNA binding and recognition by these proteins, which in turn is an important step towards the efficient design of anti-virulence agents that target these proteins. </p> </div> </div> </div>

Identification of Function and Mechanistic Insights of Guanine Deaminase fromNitrosomonas europaea: Role of the C-Terminal Loop in Catalysis

Biochemistry ◽  
2013 ◽  
Vol 52 (20) ◽  
pp. 3512-3522 ◽  
Author(s):  
Aruna Bitra ◽  
Bhukya Hussain ◽  
Ajay Singh Tanwar ◽  
Ruchi Anand
Keyword(s):  
Guanine Deaminase ◽  
Terminal Loop
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