Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate Specificity

PLoS ONE

Volumn 8, Issue 2, 2013, Pages

  Ho, Meng Chiao ^a,b   Wilczek, Carola ^a   Bonanno, Jeffrey B ^a   Xing, Li ^e   Seznec, Janina ^c   Matsui, Tsutomu ^d   Carter, Lester G ^d   Onikubo, Takashi ^a   Kumar, P Rajesh ^a   Chan, Man K ^a   Brenowitz, Michael ^a   Cheng, R Holland ^e   Reimer, Ulf ^c   Almo, Steven C ^a   Shechter, David ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^c JPT Peptide Technologies GmbH   (Germany)

^d SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^e UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; HETERODIMER; HISTONE H2A; HISTONE H4; HISTONE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN MEP50; PROTEIN PRMT5; S ADENOSYLHOMOCYSTEINE; TETRAMER; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; ELECTRON MICROSCOPY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; HISTONE ACETYLATION; HISTONE PHOSPHORYLATION; HUMAN; HUMAN CELL; MOLECULAR RECOGNITION; NONHUMAN; PEPTIDE ANALYSIS; PROTEIN PROCESSING; PROTEIN STRUCTURE; SURFACE CHARGE; XENOPUS LAEVIS;

ANIMALS; CATALYTIC DOMAIN; CHROMOSOMAL PROTEINS, NON-HISTONE; DIMERIZATION; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN-ARGININE N-METHYLTRANSFERASES; SUBSTRATE SPECIFICITY; XENOPUS LAEVIS; XENOPUS PROTEINS;

EID: 84874514092     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0057008     Document Type: Article

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