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The Human LGR7 Low‐Density Lipoprotein Class A Module Requires Calcium for Structure
Author(s) -
HOPKINS EMMA J.,
BATHGATE ROSS A.,
GOOLEY PAUL R.
Publication year - 2005
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1282.006
Subject(s) - receptor , chemistry , ldl receptor , calcium , disulfide bond , low density lipoprotein , lipoprotein , relaxin , biochemistry , biophysics , microbiology and biotechnology , biology , cholesterol , organic chemistry
A bstract : The relaxin and INSL3 receptors, LGR7 and LGR8, are the only human G‐protein‐coupled receptors to contain a low‐density lipoprotein class‐A (LDL‐A) module. LDL‐A modules are well characterized in a variety of diverse biological functions that involve ligand binding to elicit a response. Common features of the LDL‐A modules characterized to date are the conservation of three disulfide bonds and the structural arrangement around a bound calcium ion. In this study we recombinantly produce the human LGR7 LDL‐A module for NMR studies and demonstrate that calicum is required for the module to form a stable and correctly folded structure.