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PDBsum entry 4gqb
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Transferase/protein binding
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PDB id
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4gqb
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the human prmt5:mep50 complex.
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Authors
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S.Antonysamy,
Z.Bonday,
R.M.Campbell,
B.Doyle,
Z.Druzina,
T.Gheyi,
B.Han,
L.N.Jungheim,
Y.Qian,
C.Rauch,
M.Russell,
J.M.Sauder,
S.R.Wasserman,
K.Weichert,
F.S.Willard,
A.Zhang,
S.Emtage.
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Ref.
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Proc Natl Acad Sci U S A, 2012,
109,
17960-17965.
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PubMed id
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Abstract
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Protein arginine methyltransferases (PRMTs) play important roles in several
cellular processes, including signaling, gene regulation, and transport of
proteins and nucleic acids, to impact growth, differentiation, proliferation,
and development. PRMT5 symmetrically di-methylates the two-terminal ω-guanidino
nitrogens of arginine residues on substrate proteins. PRMT5 acts as part of a
multimeric complex in concert with a variety of partner proteins that regulate
its function and specificity. A core component of these complexes is the WD40
protein MEP50/WDR77/p44, which mediates interactions with binding partners and
substrates. We have determined the crystal structure of human PRMT5 in complex
with MEP50 (methylosome protein 50), bound to an S-adenosylmethionine analog and
a peptide substrate derived from histone H4. The structure of the surprising
hetero-octameric complex reveals the close interaction between the seven-bladed
β-propeller MEP50 and the N-terminal domain of PRMT5, and delineates the
structural elements of substrate recognition.
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