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Cover Feature: Kinetic Analysis of PRMT1 Reveals Multifactorial Processivity and a Sequential Ordered Mechanism (ChemBioChem 1/2018)
Author(s) -
Brown Jennifer I.,
Koopmans Timo,
van Strien Jolinde,
Martin Nathaniel I.,
Frankel Adam
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700645
Subject(s) - processivity , mechanism (biology) , chemistry , cofactor , feature (linguistics) , dimer , peptide , cover (algebra) , stereochemistry , computational biology , biology , biochemistry , physics , enzyme , philosophy , mechanical engineering , linguistics , organic chemistry , quantum mechanics , polymerase , engineering
The cover feature picture shows the cofactor SAM (teal) and the peptide binding groove (pink) within a PRMT1 dimer. We find that PRMT1 binds its substrates by using a sequential ordered mechanism in which binding of the cofactor SAM precedes binding of the target peptide similar to how putting on socks precedes putting on shoes—a handy metaphor. More information can be found in the full paper by N. I. Martin, A. Frankel et al. on page 85 in Issue 1, 2018 (DOI: 10.1002/cbic.201700521).