Sphingolipid-Binding Domain in the Serotonin1A Receptor

2012 ◽  
pp. 279-293 ◽  
Author(s):  
Amitabha Chattopadhyay ◽  
Yamuna Devi Paila ◽  
Sandeep Shrivastava ◽  
Shrish Tiwari ◽  
Pushpendra Singh ◽  
...  
Keyword(s):  
Binding Domain ◽  
Serotonin1a Receptor

Exploration of the peptide ligand-binding domain of the motilin receptor using photoaffinity labeling and receptor mutagenesis

2001 ◽  
Vol 120 (5) ◽  
pp. A509-A509
Author(s):  
B MATSUURA ◽  
M DONG ◽  
B COULIE ◽  
E HADAC ◽  
D PINON ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Photoaffinity Labeling ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Peptide Ligand ◽  
Motilin Receptor

Roles of the C-terminal peptide binding domain of human inducible HSP70 in focal ischemic brain injury

2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S53-S53
Author(s):  
Yunjuan Sun ◽  
Yibing Ouyang ◽  
Lijun Xu ◽  
Rona G Giffard
Keyword(s):  
Brain Injury ◽  
Peptide Binding ◽  
Binding Domain ◽  
Ischemic Brain Injury ◽  
Ischemic Brain

NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2.

1999 ◽  
Vol 96 (9/10) ◽  
pp. 1580-1584 ◽  
Author(s):  
I. Ségalas ◽  
S. Desjardins ◽  
H. Oulyadi ◽  
Y. Prigent ◽  
S. Tribouillard ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Peptide Fragments ◽  
Nmr Studies ◽  
Related Peptide

Limited Proteolysis of Vitronectin by Plasmin Destroys Heparin Binding Activity

1991 ◽  
Vol 66 (03) ◽  
pp. 310-314 ◽  
Author(s):  
David C Sane ◽  
Tammy L Moser ◽  
Charles S Greenberg
Keyword(s):  
Limited Proteolysis ◽  
Plasminogen Activator Inhibitor ◽  
Binding Activity ◽  
Binding Domain ◽  
Heparin Binding ◽  
Inhibitor Type ◽  
Activator Inhibitor Type ◽  
Activator Inhibitor ◽  
Pai 1

SummaryVitronectin (VN) stabilizes plasminogen activator inhibitor type 1 (PAI-1) activity and prevents the fibrin(ogen)-induced acceleration of plasminogen activation by t-PA. These antifibrinolytic activities as well as other functions are mediated by the glycosaminoglycan (GAG) binding domain of VN. Since the GAG binding region is rich in arginyl and lysyl residues, it is a potential target for enzymes such as plasmin. In this paper, the dose and time-dependent proteolysis of VN by plasmin is demonstrated. The addition of urokinase or streptokinase (200 units/ml) to plasma also produced proteolysis of VN. With minimal proteolysis, the 75 kDa band was degraded to a 62-65 kDa form of VN. This minimal proteolysis destroyed the binding of [3H]-heparin to VN and reversed the neutralization of heparin by VN.Thus, the plasmin-mediated proteolysis of the GAG binding activity of VN could destroy the antifibrinolytic activity of VN during physiologic conditions and during thrombolytic therapy. Furthermore, other functions of VN in complement and coagulation systems that are mediated by the GAG binding domain may be destroyed by plasmin proteolysis.

Ristocetin and Botrocetin Involve Two Distinct Domains of von Willebrand Factor for Binding to Platelet Membrane Glycoprotein lb

1990 ◽  
Vol 64 (02) ◽  
pp. 326-332 ◽  
Author(s):  
J P Girma ◽  
Y Takahashi ◽  
A Yoshioka ◽  
J Diaz ◽  
D Meyer
Keyword(s):  
Von Willebrand Factor ◽  
Synthetic Peptides ◽  
Competitive Inhibition ◽  
Final Concentration ◽  
Binding Domain ◽  
Platelet Membrane ◽  
Platelet Glycoprotein ◽  
Membrane Glycoprotein ◽  
Von Willebrand ◽  
Willebrand Factor

SummaryWe have evidence that ristocetin and botrocetin mediate binding of von Willebrand Factor (vWF) to platelet glycoprotein lb (GPIb) through two distinct domains on the vWF molecule. This was established by using monoclonal antibodies (MAbs) to vWF and synthetic peptides derived from the sequence of vWF. MAb 322 and MAb NMC/vW 4 both recognize native vWF as well as fragments containing the GPIb-binding domain of vWF, obtained with the following enzymes: trypsin (116 kDa), V-8 pro tease (Spill, 320 kDa) and V-8 protease plus subtilisin (33-28 kDa). Nevertheless, the lack of reciprocal displacement between the two MAbs in experiments of competitive inhibition for binding to vWF demonstrate that their respective epitopes are separate. Both MAbs inhibit 125I-vWF binding to platelet membrane GPIb and vWF-dependent platelet agglutination induced by ristocetin. However, only MAb NMC/vW4 inhibits these functions in the presence of botrocetin and when ristocetin-induced platelet agglutination is inhibited by MAb 322, botrocetin is still able to restore the agglutination. The involvement of two distinct domains of vWF for binding to GPIb in the presence of ristocetin or botrocetin was confirmed in experiments of binding of 125I-vWF to platelets using as competitor synthetic peptides corresponding to the GPIb binding domain of vWF (Cys 474 to Pro 488 and Ser 692 to Pro 708). At a final concentration of 2.5 mM both peptides inhibit more than 90% of the binding of vWF to ristocetin-treated platelets but are unable to modify this binding in the presence of botrocetin. In conclusion our data suggest that botrocetin and ristocetin involve distinct sites on vWF for binding to GPIb.

Proteomic analysis of clear cell foci in the human liver identifies differential expression of Starch-Binding Domain-Containing Protein 1 (STBD1)

2019 ◽  
Author(s):  
C Metzendorf ◽  
K Wineberger ◽  
A Cigliano ◽  
DF Calvisi ◽  
F Dombrowski ◽  
...  
Keyword(s):  
Differential Expression ◽  
Proteomic Analysis ◽  
Human Liver ◽  
Clear Cell ◽  
Binding Domain

241-LB: Positive Regulation of JAK/STAT at Signaling with SOCS3-Derived Cell-Permeable Binding Domain to ObR Induces Anti-obesity Effect

Diabetes ◽  
2020 ◽  
Vol 69 (Supplement 1) ◽  
pp. 241-LB
Author(s):  
KUYSOOK LEE ◽  
JISOOK JEON ◽  
SU JEONG KIM ◽  
HYEONTAE KANG ◽  
JEONGHUN KWAK ◽  
...  
Keyword(s):  
Binding Domain ◽  
Positive Regulation
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