Alpha Binding

Katancik JA, Sharma A, de Nardin E. Interleukin 8, neutrophil-activating peptide-2 and GRO-alpha bind to and elicit cell activation via specific and different amino acid residues of CXCR2. Cytokine 2000 12(10) 1480-1488. 

Ganju RK, Brubaker SA, Meyer J, et al. The alpha-chemokine, stromal cell-derived factor-1 alpha, binds to the transmembrane G-protein-coupled CXCR-4 receptor and activates multiple signal transduction pathways. J Biol Chem 1998 273(36) 23169-23175. 

Kohda, D., Odaka, M., Lax, I., Kawasaki, H., Suzuki, K., Ullrich, A., Schlessinger, J., and Inagaki, F. (1993). A 40-kDa epidermal growth factor/transforming growth factor alpha-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor. J. Biol. Chem. 268, 1976-1981. 

Neuschafer-Rabe F, Puschel G, Junger-mann K. 1993. Characterization of prostaglandin F2 alpha binding sites on rat hepatocyte plasma membrane. Eur. J. Biochem. 211 163-69... 

Used mainly in anesthesia protocols or in the ICU to afford muscle relaxation and/or immobility. Occasionally used to treat tetanus. These muscle relaxants interact with nicotinic receptors at the skeletal muscle end plate. Nicotinic receptors are comprised of five subunits, two of which (alpha) bind ACh, a requirement for opening of the Na+ channel. Most drugs in this class bind competitively to one of the alpha subunits to prevent depolarization (receptor antagonists) one drug (succinylcholine) binds noncompetitively and opens the Na+ channel, causing excessive depolarization and desensitization. 

Aouabdi, S., Gibson, G., and Plant, N. (2006) Transcriptional regulation of the PXR gene identification and characterization of a functional peroxisome proliferator-activated receptor alpha binding site within the proximal promoter of PXR. Drug Metab. Dispos. 34, 138-144. 

Immunomodulatory, Immunosuppresants. TNF-alpha binding antibody. Chimeric Ab composed of human constant and murine variable regions. Produced by a recombinant cell line cultured by continuous perfusion... 

Brown, M.F., Kath, J.C., and Poss, C.S. (1998) Heteroaryl-hexanoic acid amide derivatives, their preparation and their use as selective inhibitors of MlP-1-alpha binding to its CCRl receptor, W0199838167. 

D, J Sturzebecher and WBode 1991. Geometry of Binding of the N-Alpha-Tosylated Piperidides of weffl-Amidino-Phenylalanine, Para Amidino-Phenylalanine and para-Guanidino-Phenylalanine to Thrombin and Trypsin - X-ray Crystal Structures of Their Trypsin Complexes and Modeling of their Thrombin Complexes. FEBS Letters 287 133-138. 

The most frequent of the domain structures are the alpha/beta (a/P) domains, which consist of a central parallel or mixed P sheet surrounded by a helices. All the glycolytic enzymes are a/p structures as are many other enzymes as well as proteins that bind and transport metabolites. In a/p domains, binding crevices are formed by loop regions. These regions do not contribute to the structural stability of the fold but participate in binding and catalytic action. 

Figure 4.4 Schematic diagram of the structure of the a/p-barrel domain of the enzyme methylmalonyl-coenzyme A mutase. Alpha helices are red, and p strands are blue. The inside of the barrel is lined by small hydrophilic side chains (serine and threonine) from the p strands, which creates a hole in the middle where one of the substrate molecules, coenzyme A (green), binds along the axis of the barrel from one end to the other. (Adapted from a computer-generated diagram provided by P. Evans.)...

Although estrone and estradiol (26) have both been isolated from human urine, it has recently been shown that it is the latter that is the active compound that binds to the so-called estrogen receptor protein. Reduction of estrone with any of a large number of reducing agents (for example, any of the complex metal hydrides) leads cleanly to estradiol. This high degree of stereoselectivity to afford the product of attack at the alpha side of the molecule is characteristic of many reactions of steroids. 

Starting from a collection of samples remarkably well resolved (alpha > 6) on Chiralcel OD (Cellulose tris(3,5-dimethylphenylcarbamate) coated on aminopropyl silica), a putative three-point enantiophore for binding to CSR was derived (Fig. 4-10). This enantiophore query was used to search (CFS 3D search) within a list comprising 4203 compounds tested on Chiralcel OD. From this search domain of CHIRBASE 3D, 191 structures were found to match the enantiophore. 

A leucine zipper is a structural motif present in a large class of transcription factors. These dimeric proteins contain two extended alpha helices that grip the DNA molecule much like a pair of scissors at adjacent major grooves. The coiled-coil dimerization domain contains precisely spaced leucine residues which are required for the interaction of the two monomers. Some DNA-binding proteins with this general motif contain other hydrophobic amino acids in these positions hence, this structural motif is generally called a basic zipper. 

S100A1 S100 calcium binding protein A1 S100A, S 100-alpha 1q21 NM 006271... 

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