Merlin (protein)

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	==Structure==		==Structure==
−	Vertebrate merlin is a 70-[[kilodalton|kDa]] protein. There are 10 known [[isoform]]s of human merlin molecule (the full molecule being 595 [[amino acid]]s in length). The two most common these are also found in the mouse and are called ''type 1'' and ''type 2'', differing by the absence or presence of [[exon]] 16 or 17, respectively). All the known varieties have a conserved [[N-terminal]] part, which contains a [[FERM domain]] (a domain found in most cytoskeletal-membrane organizing proteins). The FERM domain is followed by an [[Alpha helix|alpha-helical]] domain and a [[hydrophilic]] tail.<ref name="pmid11756419">{{cite journal | vauthors = Shimizu T, Seto A, Maita N, Hamada K, Tsukita S, Tsukita S, Hakoshima T | title = Structural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domain | journal = J. Biol. Chem. | volume = 277 | issue = 12 | pages = 10332–6 | year = 2002 | pmid = 11756419 | doi = 10.1074/jbc.M109979200 }}</ref> Merlin can [[protein dimer|dimer]]ize with itself and heterodimerize with other ERM family proteins.	+	Vertebrate merlin is a 70-[[kilodalton|kDa]] protein. There are 10 known [[isoform]]s of human merlin molecule (the full molecule being 595 [[amino acid]]s in length). The two most common these are also found in the mouse and are called ''type 1'' and ''type 2'', differing by the absence or presence of [[exon]] 16 or 17, respectively). All the known varieties have a conserved [[N-terminal]] part, which contains a [[FERM domain]] (a domain found in most cytoskeletal-membrane organizing proteins). The FERM domain is followed by an [[Alpha helix|alpha-helical]] domain and a [[hydrophilic]] tail.<ref name="pmid11756419">{{cite journal | vauthors = Shimizu T, Seto A, Maita N, Hamada K, Tsukita S, Tsukita S, Hakoshima T | title = Structural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domain | journal = J. Biol. Chem. | volume = 277 | issue = 12 | pages = 10332–6 | year = 2002 | pmid = 11756419 | doi = 10.1074/jbc.M109979200 }}</ref><ref>{{Cite journal
		+	| pmid = 24882693
		+	| year = 2014
		+	| author1 = Ali Khajeh
		+	| first1 = J
		+	| title = Molecular conformation of the full-length tumor suppressor NF2/Merlin--a small-angle neutron scattering study.
		+	| journal = Journal of Molecular Biology
		+	| volume = 426
		+	| issue = 15
		+	| pages = 2755-68
		+	| last2 = Ju
		+	| first2 = JH
		+	| last3 = Atchiba
		+	| first3 = M
		+	| doi = 10.1016/j.jmb.2014.05.011
		+	}}</ref> Merlin can [[protein dimer|dimer]]ize with itself and heterodimerize with other ERM family proteins.
	== Function ==		== Function ==