4m36

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'''Unreleased structure'''
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{{STRUCTURE_4m36| PDB=4m36 | SCENE= }}
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===Crystal structure of Trypanosoma brucei protein arginine methyltransferase 7===
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{{ABSTRACT_PUBMED_24726341}}
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The entry 4m36 is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/ANM7_TRYB2 ANM7_TRYB2]] Arginine methyltransferase that specifically catalyzes the formation of omega-N monomethylarginine (MMA). Has activity toward multiple substrates in vitro. Able to mediate the arginine methylation of histones and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.
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Authors: Wang, C., Zhu, Y., Shi, Y.
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==About this Structure==
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[[4m36]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M36 OCA].
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Description: Crystal structure of methyltransferase 7
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==Reference==
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<ref group="xtra">PMID:024726341</ref><references group="xtra"/><references/>
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[[Category: Shi, Y.]]
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[[Category: Wang, C.]]
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[[Category: Zhu, Y.]]
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[[Category: Methyltransferase]]
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[[Category: Transferase]]

Revision as of 07:42, 23 April 2014

Template:STRUCTURE 4m36

Contents

Crystal structure of Trypanosoma brucei protein arginine methyltransferase 7

Template:ABSTRACT PUBMED 24726341

Function

[ANM7_TRYB2] Arginine methyltransferase that specifically catalyzes the formation of omega-N monomethylarginine (MMA). Has activity toward multiple substrates in vitro. Able to mediate the arginine methylation of histones and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.

About this Structure

4m36 is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Wang C, Zhu Y, Caceres TB, Liu L, Peng J, Wang J, Chen J, Chen X, Zhang Z, Zuo X, Gong Q, Teng M, Hevel JM, Wu J, Shi Y. Structural Determinants for the Strict Monomethylation Activity by Trypanosoma brucei Protein Arginine Methyltransferase 7. Structure. 2014 Apr 8. pii: S0969-2126(14)00075-6. doi:, 10.1016/j.str.2014.03.003. PMID:24726341 doi:http://dx.doi.org/10.1016/j.str.2014.03.003

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