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PDBsum entry 2mdc
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PDB id:
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Transferase
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Title:
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Solution structure of the ww domain of hypb
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Structure:
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Histone-lysine n-methyltransferase setd2. Chain: a. Fragment: unp residues 2385- 2430. Synonym: hif-1, huntingtin yeast partner b, huntingtin-interacting protein 1, hip-1, huntingtin-interacting protein b, lysine n- methyltransferase 3a, set domain-containing protein 2, hset2, p231hbp. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: hypb. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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15 models
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Authors:
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Y.G.Gao
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Key ref:
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Y.G.Gao
et al.
(2014).
Autoinhibitory structure of the WW domain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin.
Structure,
22,
378-386.
PubMed id:
DOI:
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Date:
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10-Sep-13
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Release date:
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10-Sep-14
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PROCHECK
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Headers
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References
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Q9BYW2
(SETD2_HUMAN) -
Histone-lysine N-methyltransferase SETD2 from Homo sapiens
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Seq:
Struc:
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2564 a.a.
48 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Enzyme class 2:
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E.C.2.1.1.-
- ?????
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Enzyme class 3:
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E.C.2.1.1.359
- [histone H3]-lysine(36) N-trimethyltransferase.
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Reaction:
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L-lysyl36-[histone H3] + 3 S-adenosyl-L-methionine = N6,N6,N6- trimethyl-L-lysyl36-[histone H3] + 3 S-adenosyl-L-homocysteine + 3 H+
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L-lysyl(36)-[histone H3]
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+
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3
×
S-adenosyl-L-methionine
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=
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N(6),N(6),N(6)- trimethyl-L-lysyl(36)-[histone H3]
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+
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3
×
S-adenosyl-L-homocysteine
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+
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3
×
H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Structure
22:378-386
(2014)
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PubMed id:
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Autoinhibitory structure of the WW domain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin.
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Y.G.Gao,
H.Yang,
J.Zhao,
Y.J.Jiang,
H.Y.Hu.
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ABSTRACT
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Huntington's disease (HD) is an autosomally dominant neurodegenerative disorder
caused by expansion of polyglutamine (polyQ) in the huntingtin (Htt) protein.
Htt yeast two-hybrid protein B (HYPB/SETD2), a histone methyltransferase,
directly interacts with Htt and is involved in HD pathology. Using NMR
techniques, we characterized a polyproline (polyP) stretch at the C terminus of
HYPB, which directly interacts with the following WW domain and leads this
domain predominantly to be in a closed conformational state. The solution
structure shows that the polyP stretch extends from the back and binds to the WW
core domain in a typical binding mode. This autoinhibitory structure regulates
interaction between the WW domain of HYPB and the proline-rich region (PRR) of
Htt, as evidenced by NMR and immunofluorescence techniques. This work provides
structural and mechanistic insights into the intramolecular regulation of the WW
domain in Htt-interacting partners and will be helpful for understanding the
pathology of HD.
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