scholarly journals Analysis of the conformation and ligand-binding properties of the activation segment of pig procarboxypeptidase A

1988 ◽  
Vol 251 (3) ◽  
pp. 901-905 ◽  
Author(s):  
M Vilanova ◽  
J Vendrell ◽  
C M Cuchillo ◽  
F X Avilés
Keyword(s):  
Ligand Binding ◽  
Spectral Properties ◽  
Protein Family ◽  
Binding Properties ◽  
Binding Domains ◽  
Carbocyanine Dye ◽  
Previous Hypothesis ◽  
Ef Hand ◽  
Activation Segment

The isolated activation segment of pig procarboxypeptidase A binds two Tb3+ ions in a strong and specific way. In contrast, the binding of Ca2+, Cd2+ and Mg2+ is weak. The binding of Tb3+ increases the resistance of the isolated activation segment against proteolysis and competes for the binding of the carbocyanine dye Stains-All. This dye forms complexes with the activation segment showing spectral properties similar to those observed with EF-hand structures. The presented results support a previous hypothesis on the existence of two regions in the activation segment of pancreatic procarboxypeptidases structurally related to Ca2+-binding domains of the EF-hand protein family.

scholarly journals Plastin Family of Actin-Bundling Proteins: Its Functions in Leukocytes, Neurons, Intestines, and Cancer

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Hiroto Shinomiya
Keyword(s):  
Vital Role ◽  
Protein Family ◽  
Actin Binding ◽  
Animal Cells ◽  
Cell Lineages ◽  
Binding Domains ◽  
Evolutionarily Conserved ◽  
Ef Hand ◽  
Solid Tissues ◽  
The Brain

Sophisticated regulation of the actin cytoskeleton by a variety of actin-binding proteins is essential for eukaryotic cells to perform their diverse functions. The plastin (also know, as fimbrin) protein family belongs to actin-bundling proteins, and the protein family is evolutionarily conserved and expressed in yeast, plant, and animal cells. Plastins are characterized by EF-hand Ca2+-binding domains and actin-binding domains and can cross-link actin filaments into higher-order assemblies like bundles. Three isoforms have been identified in mammals. T-plastin is expressed in cells from solid tissues, such as neurons in the brain. I-plastin expression is restricted to intestine and kidney; the isoform plays a vital role in the function of absorptive epithelia in these organs. L-plastin is expressed in hematopoietic cell lineages and in many types of cancer cells; the isoform is thus considered to be a useful biomarker for cancer.

scholarly journals Dissection of receptor folding and ligand-binding property with functional minireceptors of LDL receptor-related protein

2001 ◽  
Vol 114 (5) ◽  
pp. 899-908 ◽  
Author(s):  
L.M. Obermoeller-McCormick ◽  
Y. Li ◽  
H. Osaka ◽  
D.J. FitzGerald ◽  
A.L. Schwartz ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Ldl Receptor ◽  
Cell Surface Expression ◽  
Binding Property ◽  
Related Protein ◽  
Binding Properties ◽  
Binding Domains ◽  
Putative Ligand Binding

The LDL receptor-related protein (LRP) is a large, multifunctional endocytic receptor that binds and endocytoses a variety of structurally and functionally distinct ligands. LRP contains four putative ligand-binding domains. However, only domains II, III and IV, but not domain I, bind the receptor-associated protein (RAP), a molecular chaperone and universal antagonist for LRP. In order to dissect the function of RAP in LRP folding and to examine the ligand-binding properties of LRP, we generated LRP minireceptors that represent each of the four putative ligand-binding domains (termed mLRP1, mLRP2, mLRP3 and mLRP4, respectively). We found that proper folding and trafficking of mLRP2, mLRP3, mLRP4, but not mLRP1, is facilitated by coexpression of RAP. When these mLRPs were stably expressed in Chinese Hamster Ovary cells that lack the endogenous LRP, we found that each of these receptors was processed and traffics through the secretory pathway. Cell surface expression of these minireceptors was quantitatively examined by flow cytometric analyses. Using these minireceptor cell lines to map the ligand-binding domains, we found that although the majority of LRP ligands bind to both domain II and domain IV, Pseudomonas exotoxin A utilizes only domain IV for its binding to LRP. We conclude that while domains II and IV of LRP share many ligand-binding properties, each of the putative ligand-binding domains of LRP is unique in its contribution to ligand binding.

Ligand binding properties of the haem group

Nature ◽  
1977 ◽  
Vol 265 (5589) ◽  
pp. 15-16 ◽  
Author(s):  
A. J. Thomson
Keyword(s):  
Ligand Binding ◽  
Binding Properties

scholarly journals Paired opposing leukocyte receptors recognizing rapidly evolving ligands are subject to homogenization of their ligand binding domains

2011 ◽  
Vol 63 (12) ◽  
pp. 809-820 ◽  
Author(s):  
Sigbjørn Fossum ◽  
Per Christian Saether ◽  
John Torgils Vaage ◽  
Michael Rory Daws ◽  
Erik Dissen
Keyword(s):  
Ligand Binding ◽  
Binding Domains ◽  
Leukocyte Receptors

scholarly journals Biochemical and NMR Mapping of the Interface between CREB-binding Protein and Ligand Binding Domains of Nuclear Receptor

2004 ◽  
Vol 280 (7) ◽  
pp. 5682-5692 ◽  
Author(s):  
Fabrice A. C. Klein ◽  
R. Andrew Atkinson ◽  
Noelle Potier ◽  
Dino Moras ◽  
Jean Cavarelli
Keyword(s):  
Ligand Binding ◽  
Nuclear Receptor ◽  
Binding Protein ◽  
Creb Binding Protein ◽  
Binding Domains
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