R1526 residue in arginine/proinsulin binding domain of UGGT1 is involved in proinsulin binding

Autor:	Takeshi Imai, Jaeyong Cho, Yoji Tsugawa
Rok vydání:	2022
Předmět:	Mice Protein Folding Glucosyltransferases Biophysics Animals Insulin Cell Biology Arginine Endoplasmic Reticulum Molecular Biology Biochemistry Biophysical Phenomena Proinsulin
Zdroj:	Biochemical and biophysical research communications. 615
ISSN:	1090-2104
Popis:	Arginine releases proinsulin from binding to UGGT1 in the endoplasmic reticulum (ER). PSIPRED analysis showed that the arginine/proinsulin binding domain (A/PBD) in the C-terminal region of UGGT1 forms a disordered region, which is flexible and outside of the main protein structure. Both arginine and proinsulin may easily access the disordered region of A/PBD. Using the SNP library, two variants, Q1518∗ and R1526C, were identified in this region. UGGT1
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::589f0e8117c9fddd628b6076a238a64f https://pubmed.ncbi.nlm.nih.gov/35613513 Zobrazit plný text záznamu Full Text from ScienceDirect