title: Studies on receptor binding site of insulin: the hydrophobic B12Val can be substituted by hydrophilic thr.
abstract: [B12Thr]human insulin and [B12Leu]human insulin were obtained by means of site-directed random mutagenesis. [B12Thr]human insulin retain total biological activity but [B12Leu]human insulin has much lower biological activity. Receptor binding activities of [B12Thr]human insulin and [B12Leu]human insulin are 56% and 3%, respectively, as that of native porcine insulin. The results suggest that the hydrophobic property of the residue side chain at B12 may not be necessary.
authors.affiliation: State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry, Chinese Academy of Sciences, China.
authors.forename: Q Q
authors.initials: QQ
authors.lastname: Wang
authors.forename: Y M
authors.initials: YM
authors.lastname: Feng
authors.forename: Y S
authors.initials: YS
authors.lastname: Zhang
mesh_terms: D000818:Animals; D001665:Binding Sites; D006801:Humans; D007930:Leucine / Q000737:chemistry; D016297:Mutagenesis, Site-Directed; D010920:Placenta / Q000378:metabolism; D011384:Proinsulin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011972:Receptor, Insulin / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics; D013329:Structure-Activity Relationship; D013552:Swine; D013912:Threonine / Q000737:chemistry*; D014633:Valine / Q000737:chemistry*
chemical_list: D013912:Threonine; D011384:Proinsulin; D011972:Receptor, Insulin; D007930:Leucine; D014633:Valine