Ligand-induced conformation change in folate-binding protein
نویسندگان
چکیده
منابع مشابه
Combining quantum mechanical ligand conformation analysis and protein modeling to elucidate GPCR-ligand binding modes.
SAR beyond protein-ligand interactions: By combining structure-affinity relationships, protein-ligand modeling studies, and quantum mechanical calculations, we show that ligand conformational energies and basicity play critical roles in ligand binding to the histamine H4 receptor, a GPCR that plays a key role in inflammation.
متن کاملPSCDB: a database for protein structural change upon ligand binding
Proteins are flexible molecules that undergo structural changes to function. The Protein Data Bank contains multiple entries for identical proteins determined under different conditions, e.g. with and without a ligand molecule, which provides important information for understanding the structural changes related to protein functions. We gathered 839 protein structural pairs of ligand-free and l...
متن کاملfolate-binding protein in human blood
Synopsis The high-affinity FBP/FR (folate-binding protein/folate receptor) is expressed in three isoforms. FRα and FRβ are attached to cell membranes by hydrophobic GPI (glycosylphosphatidylinositol) anchors, whereas FBPγ is a secretory protein. Mature neutrophil granulocytes contain a non-functional FRβ on the surface, and, in addition, nanomolar concentrations of a secretory functional FBP (2...
متن کاملIngrid Remy Conformation Change Erythropoietin Receptor Activation by a Ligand - Induced
, 990 (1999); 283 Science et al. Ingrid Remy Conformation Change Erythropoietin Receptor Activation by a Ligand-Induced This copy is for your personal, non-commercial use only. clicking here. colleagues, clients, or customers by , you can order high-quality copies for your If you wish to distribute this article to others here. following the guidelines can be obtained by Permission to republish...
متن کاملImmobilized purified folate-binding protein: binding characteristics and use for quantifying folate in erythrocytes.
Purified folate-binding protein from cow's milk was immobilized on monodisperse polymer particles (Dynospheres) activated by rho-toluenesulfonyl chloride. Leakage from the spheres was less than 0.1%, and the binding properties were similar to those of the soluble protein with regard to dissociation, pH optimum for binding pteroylglutamic acid, and specificity for binding various folate derivati...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1993
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2920921