Ontology highlight
ABSTRACT:
SUBMITTER: Hoette TM
PROVIDER: S-EPMC3241878 | biostudies-literature | 2011 Dec
REPOSITORIES: biostudies-literature
Hoette Trisha M TM Clifton Matthew C MC Zawadzka Anna M AM Holmes Meg A MA Strong Roland K RK Raymond Kenneth N KN
ACS chemical biology 20111021 12
The innate immune system antibacterial protein Siderocalin (Scn) binds ferric carboxymycobactin (CMB) and also several catecholate siderophores. Although the recognition of catecholates by Scn has been thoroughly investigated, the binding interactions of Scn with the full spectrum of CMB isoforms have not been studied. Here we show that Scn uses different binding modes for the limited subset of bound CMB isoforms, resulting in a range of binding affinities that are much weaker than other siderop ...[more]