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Cracking the code of an elusive key protein modification at structural and genome scales

ABSTRACT: Characterization of Myristoylated proteins in human brain and liver samples.

INSTRUMENT(S): LTQ Orbitrap Velos, TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain, Liver

SUBMITTER: Willy Bienvenut

LAB HEAD: Dr Willy Bienvenut

PROVIDER: PXD008625 | Pride | 2018-06-18

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	140214_microsomes_H1.dat	Other
	140214_microsomes_H1.mgf	Mgf
	140214_microsomes_H1.wiff	Wiff
	140214_microsomes_H1.wiff.scan	Wiff
	140214_microsomes_H2.dat	Other

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Publications

Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern.

Castrec Benoit B Dian Cyril C Ciccone Sarah S Ebert Coralie L CL Bienvenut Willy V WV Le Caer Jean-Pierre JP Steyaert Jean-Marc JM Giglione Carmela C Meinnel Thierry T

Nature chemical biology 20180611 7

An organism's entire protein modification repertoire has yet to be comprehensively mapped. N-myristoylation (MYR) is a crucial eukaryotic N-terminal protein modification. Here we mapped complete Homo sapiens and Arabidopsis thaliana myristoylomes. The crystal structures of human modifier NMT1 complexed with reactive and nonreactive target-mimicking peptide ligands revealed unexpected binding clefts and a modifier recognition pattern. This information allowed integrated mapping of myristoylomes u ...[more]

PMID: 29892081

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