The Structural Basis of the Farnesylated and Methylated KRas4B ...
2019年11月5日 · Ca 2+ -calmodulin (CaM) extracts KRas4B from the plasma membrane, suggesting that KRas4B/CaM interaction plays a role in regulating Ras signaling.
Comparative analysis of KRAS4a and KRAS4b splice variants
2024年2月14日 · Our multidisciplinary study compared the structural and functional characteristics of KRAS4a and KRAS4b, revealing distinct structural properties and thermal stability. Position 151 influences KRAS4a’s thermal stability, while position 153 affects binding to RAF1 CRD protein.
The current understanding of KRAS protein structure and dynamics
2020年1月1日 · In this minireview, my aim is to provide the reader an overview of the publicly available KRAS structural data, insights to conformational dynamics revealed by experiments and what we have learned from MD simulations.
Structural basis of recognition of farnesylated and methylated KRAS4b …
The KRAS4b–PDEδ structure reported here provides the structural details of the protein–protein interaction interface and the atomic details of the hypervariable region of KRAS4b.
Farnesylated and methylated KRAS4b: high yield production of …
2015年11月2日 · In order to fully understand the structure and function of KRAS4b in its native environment, a high yield and high quality method for production of processed protein is essential.
Normal Mode Analysis of KRas4B Reveals Partner Specific Dynamics
2021年5月5日 · We performed normal mode analysis (NMA) of KRas4B in wild-type or mutant monomeric and neurofibromin-1 (NF1), Son of Sevenless 1 (SOS1) or Raf-1 bound dimeric conformational states to reveal partner-specific dynamics of the protein.
Substantial experimental information on the structure of membrane-bound KRAS4B has emerged only recently and points toward unrestricted conformational flexibility.
Precise Characterization of KRAS4B Proteoforms by Combining ...
Analysis of KRAS4B proteoforms by IP-TDMS provides a largely unbiased readout of PTMs with stoichiometry preserved and an improved view of global KRAS4B proteoform differences when comparing between cancer cell line or tumor contexts.
The Structural Basis of the Farnesylated and Methylated KRas4B
2019年7月11日 · Due to multiple interaction modes, we observe diverse conformational ensembles of the KRas4B–CaM complex. A highly populated conformation reveals the catalytic domain interacting with the N-lobe and the HVR wrapping around the linker with the farnesyl docking to the extended CaM’s C-lobe pocket.
Precise characterization of KRAS4b proteoforms in human ... - PNAS
2018年4月2日 · We developed an intact protein assay for the detection and quantitation of KRAS protein forms (proteoforms), enabling the measurement of how genetically encoded mutations affect posttranslational modifications on the same protein molecule.
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