Ontology highlight
ABSTRACT:
SUBMITTER: Yuan Y
PROVIDER: S-EPMC6983471 | biostudies-literature | 2019 Oct
REPOSITORIES: biostudies-literature
Yuan Yue Y Ayinuola Yetunde A YA Singh Damini D Ayinuola Olawole O Mayfield Jeffrey A JA Quek Adam A Whisstock James C JC Law Ruby H P RHP Lee Shaun W SW Ploplis Victoria A VA Castellino Francis J FJ
Journal of structural biology 20190710 1
VEK50 is a truncated peptide from a Streptococcal pyogenes surface human plasminogen (hPg) binding M-protein (PAM). VEK50 contains the full A-domain of PAM, which is responsible for its low nanomolar binding to hPg. The interaction of VEK50 with kringle 2, the PAM-binding domain in hPg (K2<sub>hPg</sub>), has been studied by high-resolution NMR spectroscopy. The data show that each VEK50 monomer in solution contains two tight binding sites for K2<sub>hPg</sub>, one each in the a1- (RH1; R<sup>17 ...[more]