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Article

Structural basis for substrate recognition by the human N-terminal methyltransferase 1.

Genes & development - 15 Nov 2015

Dong Cheng, Mao Yunfei, Tempel Wolfram, Qin Su, Li Li, Loppnau Peter, Huang Rong, Min Jinrong

Abstract excerpt

α-N-terminal methylation represents a highly conserved and prevalent post-translational modification, yet its biological function has remained largely speculative. The recent discovery of α-N-terminal methyltransferase 1 (NTMT1) and its physiological substrates propels the elucidation of a general role of α-N-terminal methylation in mediating DNA-binding ability of the modified proteins. The phenotypes, observed...

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Share to Amino Acid Motifs
Share to Crystallization
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Knockdown Techniques

Share to Methylation

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Source

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Identifiers

PMID: 26543161
DOI: 10.1101/gad.270611.115
PMCID: PMC4691889

Genes

NTMT1

Provenance

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