Considering both small and large scale motions of vascular endothelial growth factor (VEGF) is crucial for reliably predicting its binding affinities to DNA aptamers.

ABSTRACT: Vascular endothelial growth factor 165 (VEGF₁₆₅), a predominant isoform of VEGF signal proteins, is an ideal target for developing drugs against various diseases. It is composed of a heparin binding domain (HBD) and a receptor binding domain (RBD), which are connected by a flexible linker. Among the two domains, RBD is utilized in binding with the signal transduction protein, the VEGF receptor (VEGFR). None the less for its pharmaceutical importance, structure-based studies for developing drugs has been severely hindered by the lack of its whole structure determination, mainly owing to the existence of the flexible linker. Fortunately, the utilization of computer simulation methods can offer a possibility to circumvent this difficult issue. Here, we employ ensemble docking in co

SUBMITTER: Lee W 

PROVIDER: S-EPMC8695334 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature