Remodeling KRAS

Daniel J Deredge; Patrick L Wintrode

doi:10.1016/j.str.2017.08.012

Remodeling KRAS

Structure. 2017 Sep 5;25(9):1323-1324. doi: 10.1016/j.str.2017.08.012.

Authors

Daniel J Deredge¹, Patrick L Wintrode²

Affiliations

¹ Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, 20 North Pine St., Baltimore, MD 21201, USA.
² Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, 20 North Pine St., Baltimore, MD 21201, USA. Electronic address: [email protected].

PMID: 28877504
DOI: 10.1016/j.str.2017.08.012

Abstract

Mutations in members of the RAS family of small GTPases have been associated with numerous human cancers. However, RAS family members are notoriously difficult to target. In this issue of Structure, Lu et al. (2017) examine the effects of two compounds with distinct chemical scaffolds on the structure and dynamics of an oncogenic KRAS mutant, thus highlighting the usefulness of HDX-MS for drug development.

Publication types

Comment

MeSH terms

Deuterium
Humans
Hydrogen
Mass Spectrometry
Mutation
Proto-Oncogene Proteins p21(ras) / genetics*
ras Proteins / genetics*

Substances

KRAS protein, human
Hydrogen
Deuterium
Proto-Oncogene Proteins p21(ras)
ras Proteins