2021年1月1日 · Human serum albumin (HSA) is the major protein component of human plasma. The structure of HSA consists of three homologous α-helical domains (domains I, II and III) [1, 2] comprising six-helix and four-helix subdomains (subdomains A and B) [2, 3] and contains multiple cavities where numerous kinds of ligands can bind.

We have now determined the crystal structure of HSA complexed with five molecules of myristate at 2.5 Å resolution. The fatty acid molecules bind in long, hydrophobic pockets capped by polar...

1997年7月18日 · A new triclinic crystal form of human serum albumin (HSA), derived either from pool plasma (pHSA) or from a Pichia pastoris expression system (rHSA), was obtained from polyethylene glycol 4000 solution.

With overgrowing applications in hybridoma culture media, stem cell culture media, and tissue engineering media, albumins are becoming more relevant to modern-day bioprocess development. High-resolution structures of HSA have identified critical residues for ligand binding and transport, which are essential for the growth and development of cells.

2 天之前 · The interaction between TBBPS-BME and HSA results in changes in HSA's conformation, leading to a decrease in α-helix proportion and an overall loosening of the protein structure. The presence of TBBPS-BME may influence the esterase-like activity of HSA, potentially through interactions involving residues Lys199 and Lys195, as suggested by ...

2014年9月21日 · HSA structures. The coordinates of different structures of HSA deposited in PDB were obtained from X-ray crystallography. More than 50 structures can be found. Each structure corresponds to the HSA under different experimental conditions, either unbound or bound to diverse ligands (mainly anesthetics and fatty acids).

2019年2月15日 · Human serum albumin (HSA) is an opulent, non-glycosylated, most versatile carrier protein in plasma possessing multiple functions. HSA has the ability to interact with a variety of ligands, including exogenous pharmacological drugs. HSA has multiple binding sites located in different subdomains and which are responsible for binding of ligands.

2003年7月7日 · The structure of the HSA-hemin-myristate complex (PDB ID 1o9x) reveals the key polar and hydrophobic interactions that determine the hemin-binding specificity of HSA. The details of the hemin-binding environment of HSA provide a structural foundation for efforts to modify the protein and/or the heme molecule in order to engineer complexes that ...

Human serum albumin (HSA) is the most abundant protein in plasma, and plays multiple roles in physiology, including as a carrier protein for endogenous and exogenous compounds. Recent studies provide new evidences to support the enzymatic activities of HSA and new molecular insights for such activit …

Human serum albumin (HSA) plays an important role in the transference of pharmaceuticals, hormones, and fatty acids, along with other compounds, determining their...