Ontology highlight
ABSTRACT:
SUBMITTER: Li HY
PROVIDER: S-EPMC4861447 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Li Hai-Yun HY Wang Jing J Meng Fan F Jia Zhe-Kun ZK Su Yang Y Bai Qi-Feng QF Lv Ling-Ling LL Ma Fu-Rong FR Potempa Lawrence A LA Yan Yong-Bin YB Ji Shang-Rong SR Wu Yi Y
The Journal of biological chemistry 20160223 16
Most proinflammatory actions of C-reactive protein (CRP) are only expressed following dissociation of its native pentameric assembly into monomeric form (mCRP). However, little is known about what underlies the greatly enhanced activities of mCRP. Here we show that a single sequence motif, i.e. cholesterol binding sequence (CBS; a.a. 35-47), is responsible for mediating the interactions of mCRP with diverse ligands. The binding of mCRP to lipoprotein component ApoB, to complement component C1q, ...[more]