4ZRI: Merlin-FERM and Lats2

Crystal structure of Merlin-FERM and Lats2. Determined by X-ray diffraction at 2.7 Å resolution. Released 17 Jun 2015.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,975
Mol. weight: 83.09 kDa
Released: 17 Jun 2015

Explore 4ZRI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ZRI contains 26 α-helices and 34 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 12 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	21-27	7	1
β-strand	32-38	7	1
β-strand	42	1	2
α-helix	43-54	12
α-helix	59-61	3
β-strand	62-68	7	1
β-strand	71-74	4	1
β-strand	80	1	2
α-helix	81-83	3
β-strand	92-98	7	1
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-174	4
β-strand	177	1	3
α-helix	181-194	14
α-helix	200-211	12
β-strand	220-226	7	4
β-strand	231-236	6	4
β-strand	240-244	5	4
β-strand	254-257	4	4
α-helix	258-260	3
β-strand	261-266	6	4
β-strand	270-275	6	4
α-helix	281-282	2
β-strand	283-286	4	4
α-helix	290-310	21

Chain B: 11 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	22-27	6	5
β-strand	32-37	6	5
β-strand	42	1	6
α-helix	43-54	12
α-helix	59-61	3
β-strand	62-68	7	5
β-strand	71-74	4	5
β-strand	80	1	6
β-strand	92-98	7	5
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-174	4
β-strand	177	1	7
α-helix	181-193	13
α-helix	200-211	12
β-strand	220-225	6	8
β-strand	231-236	6	8
β-strand	240-244	5	8
β-strand	245	1	9
β-strand	248	1	9
β-strand	254-257	4	8
α-helix	258-260	3
β-strand	261-267	7	8
β-strand	270-275	6	8
α-helix	281-282	2
β-strand	283-286	4	8
α-helix	290-309	20

Chain C: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	74-84	11
α-helix	85-87	3
β-strand	88	1	3

Chain D: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	74-84	11
β-strand	88	1	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Merlin	A, B	protein	324	Homo sapiens	P35240 (AlphaFold model)
Serine/threonine-protein kinase LATS2	C, D	protein	32	Homo sapiens	Q9NRM7 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4ZRI_1 Merlin (chains A, B)
GPGSMAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGL
RETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQH
LFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINL
YQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGV
DALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLI
LQLCIGNHDLFMRRRKADSLEVQQ

Sequence of entity 2 (C, D), FASTA

>4ZRI_2 Serine/threonine-protein kinase LATS2 (chains C, D)
PKFGPYQKALREIRYSLLPFANESGTSAAAEV

Primary citation

Angiomotin binding-induced activation of Merlin/NF2 in the Hippo pathway. Li, Y., Zhou, H., Li, F. et al. Cell Res (2015) 25:801-817. DOI 10.1038/cr.2015.69 · PubMed

Other PDB entries of the same protein (UniProt P35240 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7LWH 1.61 Å, Human neurofibromin 2/merlin residues 1-339 in complex with LATS1
1H4R 1.8 Å, Crystal Structure of the FERM domain of Merlin, the Neurofibromatosis 2 Tumor Suppressor…
4ZRJ 2.3 Å, Structure of Merlin-FERM and CTD
6CDS 2.62 Å, Human neurofibromin 2/merlin/schwannomin residues 1-339 in complex with PIP2
3U8Z 2.64 Å, human merlin FERM domain

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