Histidine146 of Human Serum Albumin Plays a Prominent Role at the Interface of Subdomains IA and IIA in Allosteric Ligand Binding

Histidine146 of Human Serum Albumin Plays a Prominent Role at the Interface of Subdomains IA and IIA in Allosteric Ligand Binding

Fatty acids are endogenous ligands of human serum albumin (HSA) that induce conformational changes and participate in allosteric ligand binding to HSA. In a previous study, we showed that, when myristate (MYR) is present, the binding of [14C]ketoprofen (KP) to subdomain IA of HSA was increased, indi...

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Bibliographic Details
Main Authors: Kaneko, K., Chuang, Victor, Minomo, A., Yamasaki, K., Bhagavan, N., Maruyama, T., Otagiri, M.
Format: Journal Article
Published: Wiley 2011
Subjects:
allosteric ligand binding
N-B transition
human serum albumin
photoaffinity labeling
histidine
Online Access:http://hdl.handle.net/20.500.11937/38202

Internet

http://hdl.handle.net/20.500.11937/38202

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