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Structural dynamics of the receptor-binding domain of colicin E9

Faraday Discussions, 2002
Colicin E9 is a 61 kDa antibacterial protein secreted by E. coli. In order for it to enter the cytoplasm of susceptible bacteria and kill them by hydrolysing their DNA, the colicin must first interact with an outer membrane receptor on the target cell, BtuB, and a translocation pathway involving Tol proteins.
Boetzel, Ruth   +5 more
openaire   +3 more sources

Homology modeling of the receptor binding domain of human thrombopoietin

Journal of Computer-Aided Molecular Design, 1998
Platelet production in blood is regulated by a lineage specific humoral factor, thrombopoietin (TPO). The amino terminal domain of TPO (TPO-N) is responsible for the signal transduction mediated by the TPO receptor, c-mpl. From the predicted length of helices we found that TPO-N belongs to the long-chain subfamily of the four-helix bundle cytokine ...
Jin-Soo Song   +4 more
openaire   +2 more sources

Definition of Receptor Binding Domains in Interferon-α

Journal of Interferon Research, 1992
Earlier studies from this laboratory had identified three regions in interferon-alpha (IFN-alpha) that influence the active conformation of the molecule. These domains are associated with the amino acid residues 10-35, 78-107, and 123-166. In this report, we define these domains more accurately by identifying their critical clusters of amino acids ...
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Topology of receptor binding domains of mouse IFN- gamma .

The Journal of Immunology, 1990
Abstract IFN-gamma is an essential immunoregulatory lymphokine for a variety of immunologic functions including upregulation of MHC Ag. The elucidation of the structure, particularly the receptor binding domains, should further enhance our understanding of its mechanism of action, and provide a rational basis for modulation of its ...
M A, Jarpe, H M, Johnson
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Crystallization of the receptor binding domain of vascular endothelial growth factor

Proteins: Structure, Function, and Genetics, 1996
Vascular endothelial growth factor (VEGF) is a potent angiogenic factor with a unique specificity for vascular endothelial cells. In addition to its role in vasculogenesis and embryonic angiogenesis, VEGF is implicated in pathologic neovascularization associated with tumors and diabetic retinopathy.
H W, Christinger   +6 more
openaire   +2 more sources

Biophysical analysis of the EPEC translocated intimin receptor-binding domain

Biochemical and Biophysical Research Communications, 2007
Enteropathogenic Escherichia coli (EPEC) are Gram (-) bacteria responsible for widespread illness in the form of diarrhea. EPEC cells attach to the intestinal epithelium using a Type III secretion system common to many Gram (-) bacteria. The translocated intimin receptor (TIR) is the first protein secreted through the EPEC secretion complex, and is ...
Nathan T, Ross   +2 more
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Platelet Activation by the apoB/E Receptor-binding Domain of LDL

Thrombosis and Haemostasis, 2002
SummaryLow density lipoprotein (LDL) increases the sensitivity of human platelets for agonists by activating p38MAPK. Antibody 4G3 disturbs apoB100 binding to the classical apoB/E receptor and inhibits LDLinduced p38MAPK activation, whereas an antibody against a distal domain on apoB100 has no effect.
A M, Relou   +3 more
openaire   +2 more sources

Structural insights into the receptor-binding domain of bat coronavirus ZXC21

Structure
Bat coronaviruses ZXC21 and ZC45 were discovered before the COVID-19 outbreak and share approximately 86% genome homology with SARS-CoV-2. Earlier studies indicated that ZXC21 and ZC45 may be involved in the emergence of SARS-CoV-2. However, the cell invasion mechanisms of ZXC21 and ZC45 remain unclear.
Chenghai, Wang   +5 more
openaire   +2 more sources

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