Literature summary for 2.1.1.348 extracted from

Wang, X.; Feng, J.; Xue, Y.; Guan, Z.; Zhang, D.; Liu, Z.; Gong, Z.; Wang, Q.; Huang, J.; Tang, C.; Zou, T.; Yin, P.
Structural basis of N(6)-adenosine methylation by the METTL3-METTL14 complex (2016), Nature, 534, 575-578 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of the METTL3-METTL14 heterodimer with methyltransferase domains in the ligand-free, S-adenosyl methionine (AdoMet-)bound and S-adenosyl homocysteine (AdoHcy-)bound states, with resolutions of 1.9, 1.71 and 1.61 A, respectively. Both METTL3 and METTL14 adopt a class I methyltransferase fold and they interact with each other via an extensive hydrogen bonding network, generating a positively charged groove	Homo sapiens

Crystallization (Comment)

Organism

crystal structures of the METTL3-METTL14 heterodimer with methyltransferase domains in the ligand-free, S-adenosyl methionine (AdoMet-)bound and S-adenosyl homocysteine (AdoHcy-)bound states, with resolutions of 1.9, 1.71 and 1.61 A, respectively. Both METTL3 and METTL14 adopt a class I methyltransferase fold and they interact with each other via an extensive hydrogen bonding network, generating a positively charged groove

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q86U44 and Q9HCE5	Q86U44 i.e. catalytic subunit METTL3, Q9HCE5 i.e non-catalytic subunit METTL14	-

General Information

General Information	Comment	Organism
physiological function	in the m6A methyltransferase complex, METTL3 primarily functions as the catalytic core, while METTL14 serves as an RNA-binding platform	Homo sapiens

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Release 2023.1 (January 2023)