Structures of N-terminally processed KRAS provide insight into the role of N-acetylation.
Acetylation
Amino Acid Sequence
Catalytic Domain
Crystallography, X-Ray
Guanosine Diphosphate
/ metabolism
Guanylyl Imidodiphosphate
/ metabolism
Humans
Hydrogen Bonding
Magnesium
/ metabolism
Models, Molecular
Protein Binding
Protein Conformation
Protein Processing, Post-Translational
Proto-Oncogene Proteins p21(ras)
/ chemistry
Sequence Alignment
Sequence Homology, Amino Acid
Structure-Activity Relationship
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
19 07 2019
19 07 2019
Historique:
received:
16
10
2018
accepted:
04
07
2019
entrez:
21
7
2019
pubmed:
22
7
2019
medline:
3
11
2020
Statut:
epublish
Résumé
Although post-translational modification of the C-terminus of RAS has been studied extensively, little is known about N-terminal processing. Mass spectrometric characterization of KRAS expressed in mammalian cells showed cleavage of the initiator methionine (iMet) and N-acetylation of the nascent N-terminus. Interestingly, structural studies on GDP- and GMPPNP-bound KRAS lacking the iMet and N-acetylation resulted in Mg
Identifiants
pubmed: 31324887
doi: 10.1038/s41598-019-46846-w
pii: 10.1038/s41598-019-46846-w
pmc: PMC6642148
doi:
Substances chimiques
KRAS protein, human
0
Guanosine Diphosphate
146-91-8
Guanylyl Imidodiphosphate
34273-04-6
HRAS protein, human
EC 3.6.5.2
Proto-Oncogene Proteins p21(ras)
EC 3.6.5.2
Magnesium
I38ZP9992A
Types de publication
Comparative Study
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
10512Subventions
Organisme : CCR NIH HHS
ID : HHSN261200800001C
Pays : United States
Organisme : NCI NIH HHS
ID : HHSN261200800001E
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM103403
Pays : United States
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