Ligand Binding Sites of Inducible Costimulator and High Avidity Mutants with Improved Function

Receptor Binding Site of the Protein State and Functional Mapping of the Determination of the Cell Surface Oligomeric Ligand Costimulatory Function: Structural Basis of Inducible Costimulator

Interaction of Human Serum Albumin with Ethyl 2-[2-(dimethylamino)-4-(4-nitrophenyl)-1,3-thiazole-5-yl]-2-oxoacetate as a Synthesized Ligand

The interaction of human serum albumin with Ethyl 2-[2-(dimethylamino)-4-(4-nitrophenyl)- 1,3-thiazole-5-yl]-2-oxoacetate was investigated by using isothermal titration UV-visible spectrophotometry in tris-buffer, pH 7.4. According to these results, it was found that there are a set of 4 binding sites for this ligand on HSA with positive cooperativity in the binding process. This thiazole deriv...

P-30: The Effect of The T26248G Polymorphism on Putative MethyltransferaseNsun7 Protein Function and Its Role in Male Infertility

Background: Male infertility has many causes, including genetic infertility. The NOP2/Sun domain family, member7 (Nsun7) gene, which encodes putative methyltransferase Nsun7, has a role in sperm motility. The aim of the present study was to investigate the effect of the T26248G polymorphism on Nsun7 protein function and its role in male infertility. Materials and Methods: Semen samples were col...

P-31: The Alteration of SpermatogenesisHas A Correlation with Sertoli Cell Mitochondrial Abnormal Morphology in Cytotoxicity of Testicular Tissue Mediatedwith Monosodium

Background: Male infertility has many causes, including genetic infertility. The NOP2/Sun domain family, member7 (Nsun7) gene, which encodes putative methyltransferase Nsun7, has a role in sperm motility. The aim of the present study was to investigate the effect of the T26248G polymorphism on Nsun7 protein function and its role in male infertility. Materials and Methods: Semen samples were col...

Probing the phosphocholine-binding site of human C-reactive protein by site-directed mutagenesis.

Human C-reactive protein (CRP) can activate the classical pathway of complement and function as an opsonin only when it is complexed to an appropriate ligand. Most known CRP ligands bind to the phosphocholine (PCh)-binding site of the protein. In the present study, we used oligonucleotide-directed site-specific mutagenesis to investigate structural determinants of the PCh-binding site of CRP. E...