DNA condensation by high-affinity interaction with avidin

2004 ◽  
Vol 17 (6) ◽  
pp. 558-566 ◽  
Author(s):  
Margherita Morpurgo ◽  
Aurelian Radu ◽  
Edward A. Bayer ◽  
Meir Wilchek
Keyword(s):  
Dna Condensation ◽  
High Affinity ◽  
Affinity Interaction

scholarly journals Molecular Basis for the High Affinity Interaction between the Thymic Leukemia Antigen and the CD8αα Molecule

2005 ◽  
Vol 174 (6) ◽  
pp. 3501-3507 ◽  
Author(s):  
Antoine Attinger ◽  
Lesley Devine ◽  
Yiran Wang-Zhu ◽  
Donald Martin ◽  
Jia-huai Wang ◽  
...  
Keyword(s):  
Molecular Basis ◽  
High Affinity ◽  
Affinity Interaction ◽  
Leukemia Antigen

High level expression of the Drosophila Toll receptor ectodomain and crystallization of its complex with the morphogen Spätzle

2013 ◽  
Vol 394 (8) ◽  
pp. 1091-1096 ◽  
Author(s):  
Marco Stelter ◽  
Uwe Fandrich ◽  
Kati Franzke ◽  
Angelika Schierhorn ◽  
Constanze Breithaupt ◽  
...  
Keyword(s):  
Immune Response ◽  
High Level Expression ◽  
Receptor Ligand ◽  
High Affinity ◽  
Cystine Knot ◽  
Toll Receptor ◽  
Cystine Knot Protein ◽  
High Yields ◽  
High Level ◽  
Affinity Interaction

Abstract Drosophila Toll receptors are involved in embryonic development and in the immune response of adult flies. In both processes, the Toll receptor ligand is the NGF-like cystine knot protein Spätzle. Here we present the expression of Toll receptor ectodomain in Schneider cells at high yields and demonstrate a high affinity interaction with the refolded and trypsin-processed Spätzle cystine knot domain dimer. Poorly and anisotropically diffracting crystals of the complex could be improved by deglycosylation and dehydration, paving the way for structural analyses of the Toll-Spätzle interaction.

Expression phenotypes suggest that Der participates in a specific, high affinity interaction with membranes

2011 ◽  
Vol 78 (1) ◽  
pp. 102-112 ◽  
Author(s):  
Ryan Lee ◽  
May Thandar Aung-Htut ◽  
Charlotte Kwik ◽  
Paul E. March
Keyword(s):  
High Affinity ◽  
Affinity Interaction

scholarly journals GPVI (Glycoprotein VI) Interaction With Fibrinogen Is Mediated by Avidity and the Fibrinogen αC-Region

2021 ◽  
Vol 41 (3) ◽  
pp. 1092-1104
Author(s):  
Rui-Gang Xu ◽  
Julia S. Gauer ◽  
Stephen R. Baker ◽  
Alexandre Slater ◽  
Eleyna M. Martin ◽  
...  
Keyword(s):  
Molecular Level ◽  
Dissociation Rate ◽  
Fibrin Polymerization ◽  
Downstream Signaling ◽  
Protein Protein Interaction ◽  
Glycoprotein Vi ◽  
High Affinity ◽  
Platelet Signaling ◽  
Dimeric Form ◽  
Affinity Interaction

Objective: GPVI (glycoprotein VI) is a key molecular player in collagen-induced platelet signaling and aggregation. Recent evidence indicates that it also plays important role in platelet aggregation and thrombus growth through interaction with fibrin(ogen). However, there are discrepancies in the literature regarding whether the monomeric or dimeric form of GPVI binds to fibrinogen at high affinity. The mechanisms of interaction are also not clear, including which region of fibrinogen is responsible for GPVI binding. We aimed to gain further understanding of the mechanisms of interaction at molecular level and to identify the regions on fibrinogen important for GPVI binding. Approach and Results: Using multiple surface- and solution-based protein-protein interaction methods, we observe that dimeric GPVI binds to fibrinogen with much higher affinity and has a slower dissociation rate constant than the monomer due to avidity effects. Moreover, our data show that the highest affinity interaction of GPVI is with the αC-region of fibrinogen. We further show that GPVI interacts with immobilized fibrinogen and fibrin variants at a similar level, including a nonpolymerizing fibrin variant, suggesting that GPVI binding is independent of fibrin polymerization. Conclusions: Based on the above findings, we conclude that the higher affinity of dimeric GPVI over the monomer for fibrinogen interaction is achieved by avidity. The αC-region of fibrinogen appears essential for GPVI binding. We propose that fibrin polymerization into fibers during coagulation will cluster GPVI through its αC-region, leading to downstream signaling, further activation of platelets, and potentially stimulating clot growth. Graphic Abstract: A graphic abstract is available for this article.

scholarly journals Cytosolic protein binding to band-3 protein inhibits endocytosis of isolated human erythrocyte membranes

1982 ◽  
Vol 207 (3) ◽  
pp. 595-598 ◽  
Author(s):  
K A Cordes ◽  
J M Salhany
Keyword(s):  
Membrane Protein ◽  
Integral Membrane Protein ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Band 3 Protein ◽  
High Affinity ◽  
Human Erythrocyte Membranes ◽  
Affinity Interaction ◽  
Cytoplasmic Side

Recent studies of haemoglobin binding to the cytoplasmic side of the erythrocyte membrane have shown that the predominant high-affinity interaction occurs with the major integral membrane protein known as band-3 protein and that this interaction may occur within the intact erythrocyte in a manner regulated by cell pH. We report here that haemoglobin and glyceraldehyde 3-phosphate dehydrogenase binding to band-3 protein in isolated membranes can inhibit endocytosis during vesiculation in vitro. The specificity of this effect was demonstrated by showing that myoglobin, which has an affinity for the membrane fully one to two orders of magnitude lower than that for haemoglobin, does not inhibit endocytosis.

scholarly journals p120-Catenin Is a Key Component of the Cadherin–γ-Secretase Supercomplex

2008 ◽  
Vol 19 (10) ◽  
pp. 4042-4050 ◽  
Author(s):  
Alexi Kiss ◽  
Regina B. Troyanovsky ◽  
Sergey M. Troyanovsky
Keyword(s):  
Proteolytic Activity ◽  
Cell Contact ◽  
Compelling Evidence ◽  
P120 Catenin ◽  
Low Level ◽  
High Affinity ◽  
Affinity Interaction ◽  
E Cadherin ◽  
Cell Cell

In this work, we show several previously unknown features of p120-catenin in a cadherin–catenin complex that are critical for our understanding of cadherin-based adhesion and signaling. We show that in human epithelial A-431 cells, nearly all p120 molecules engage in high-affinity interaction with E-cadherin–catenin complexes located at the cellular surface. p120 is positioned in proximity to α-catenin in the complex with cadherin. These findings suggest a functional cooperation between p120 and α-catenin in cadherin-based adhesion. A low level of cadherin-free p120 molecules, in contrast, could facilitate p120-dependent signaling. Finally, we present compelling evidence that p120 is a key linker cementing the E-cadherin–catenin complex with the transmembrane protease γ-secretase. The cell–cell contact location of this supercomplex makes it an important candidate for conducting different signals that rely on γ-secretase proteolytic activity.

scholarly journals Regions outside of conserved PxxPxR motifs drive the high affinity interaction of GRB2 with SH3 domain ligands

2015 ◽  
Vol 1853 (10) ◽  
pp. 2560-2569 ◽  
Author(s):  
Rebekah R. Bartelt ◽  
Jonathan Light ◽  
Aldo Vacaflores ◽  
Alayna Butcher ◽  
Madhana Pandian ◽  
...  
Keyword(s):  
Sh3 Domain ◽  
High Affinity ◽  
Affinity Interaction

Fc Engineering: Tailored Synthetic Human IgG1-Fc Repertoire for High-Affinity Interaction with FcRn at pH 6.0

2018 ◽  
pp. 399-417
Author(s):  
Abhishek Saxena ◽  
Bingxin Bai ◽  
Shin-Chen Hou ◽  
Lianlian Jiang ◽  
Tianlei Ying ◽  
...  
Keyword(s):  
High Affinity ◽  
Human Igg1 ◽  
Affinity Interaction
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