2020
DOI: 10.1101/2020.08.14.250738
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Long-lasting salt bridges provide the anchoring mechanism of oncogenic KRas-4B proteins at cell membranes

Abstract: Ras is a family of related proteins participating in all animal cell lineages and organs which work as GDP-GTP binary switches and regulate cytoplasmic signalling networks able to control several cellular processes, playing an essential role in signal transduction pathways involved in cell growth, differentiation and survival. In this work, a G12D mutated farnesylated GTP bound KRas-4B protein has been simulated at the interface of a DOPC/DOPS/cholesterol model anionic cell membrane at the all-atom level. A sp… Show more

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Cited by 1 publication
(5 citation statements)
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“…So increasing the temperature of the system leads to an increased area per lipid of certain phosphatidylcholine lipids as it was observed for temperatures below 420 K [53]. It was previously reported that KRas-4B can interact with head groups of DOPC and DOPS lipid molecules through long-lived salt bridges and hydrogen-bonds [21]. Accordingly, when the system temperature rises, for the same model membrane, its thickness decreases.…”
Section: Area Per Lipidmentioning
confidence: 55%
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“…So increasing the temperature of the system leads to an increased area per lipid of certain phosphatidylcholine lipids as it was observed for temperatures below 420 K [53]. It was previously reported that KRas-4B can interact with head groups of DOPC and DOPS lipid molecules through long-lived salt bridges and hydrogen-bonds [21]. Accordingly, when the system temperature rises, for the same model membrane, its thickness decreases.…”
Section: Area Per Lipidmentioning
confidence: 55%
“…As is described in Ref. [21], the FAR of the wild-type KRas-4B-Far is revealed to be able to anchor into and depart from the membrane without difficulty in the chol.-30% case when GTP favors binding with the interface of the membrane through salt-bridges and hydrogen-bonds, located at around 2.39 nm from the membrane center. The FAR can have two preferred localisations: 1) 3.90 nm when FAR wanders in the water region, and 2) 1.73 nm when FAR anchors inside of the PM.…”
Section: Preferential Localization Of Kras-4b-far On Membranesmentioning
confidence: 56%
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