3WA0: Merlin

Crystal structure of merlin complexed with DCAF1/VprBP. Determined by X-ray diffraction at 2.31 Å resolution. Released 28 May 2014.

Method: X-ray diffraction
Resolution: 2.31 Å
Organisms: Mus musculus, Homo sapiens
Chains: 11
Atoms: 15,373
Mol. weight: 235.92 kDa
Released: 28 May 2014

Explore 3WA0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3WA0 contains 70 α-helices and 90 β-strands across 11 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: 11 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	25-27	3	1
β-strand	32-34	3	1
β-strand	42	1	2
α-helix	43-54	12
β-strand	62-68	7	1
β-strand	71-74	4	1
β-strand	80	1	2
α-helix	81-83	3
α-helix	92	1
β-strand	93-98	6	1
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-175	5
α-helix	181-193	13
α-helix	200-211	12
β-strand	220-226	7	3
β-strand	231-237	7	3
β-strand	240-244	5	3
β-strand	254-257	4	3
α-helix	258-260	3
β-strand	261-267	7	3
β-strand	270-275	6	3
β-strand	283-286	4	3
α-helix	290-310	21

Chain B: 11 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	24-27	4	4
β-strand	32-35	4	4
β-strand	42	1	5
α-helix	43-54	12
β-strand	62-68	7	4
β-strand	71-74	4	4
β-strand	80	1	5
α-helix	81-83	3
β-strand	92-98	7	4
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-176	6
α-helix	181-194	14
α-helix	200-211	12
α-helix	219	1
β-strand	220-225	6	6
β-strand	231-237	7	6
β-strand	240-244	5	6
β-strand	254-257	4	6
α-helix	258-260	3
β-strand	261-267	7	6
β-strand	270-275	6	6
β-strand	283-286	4	6
α-helix	290-311	22

Chain C: 13 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	22-27	6	7
β-strand	32-37	6	7
β-strand	42	1	8
α-helix	43-54	12
β-strand	62-68	7	7
β-strand	71-74	4	7
β-strand	80	1	8
α-helix	81-83	3
β-strand	92-98	7	7
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-175	5
α-helix	181-192	12
α-helix	193-195	3
α-helix	200-211	12
α-helix	219	1
β-strand	220-225	6	9
β-strand	231-236	6	9
β-strand	240-244	5	9
β-strand	254-257	4	9
α-helix	258-260	3
β-strand	261-267	7	9
β-strand	270-275	6	9
α-helix	281-282	2
β-strand	283-286	4	9
α-helix	290-310	21

Chain D: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	21-27	7	10
β-strand	32-38	7	10
β-strand	42	1	11
α-helix	43-54	12
β-strand	62-68	7	10
β-strand	71-74	4	10
β-strand	80	1	11
α-helix	81-83	3
β-strand	92-98	7	10
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-174	4
α-helix	181-192	12
α-helix	193-195	3
α-helix	200-211	12
β-strand	220-225	6	12
β-strand	231-237	7	12
β-strand	240-244	5	12
β-strand	254-257	4	12
α-helix	258-260	3
β-strand	261-267	7	12
β-strand	270-275	6	12
α-helix	281-282	2
β-strand	283-286	4	12
α-helix	290-312	23

Chain E: 12 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	22-27	6	13
β-strand	32-37	6	13
β-strand	42	1	14
α-helix	43-54	12
β-strand	62-67	6	13
β-strand	72-74	3	13
β-strand	80	1	14
α-helix	81-83	3
β-strand	92-98	7	13
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-174	4
α-helix	181-193	13
α-helix	200-211	12
α-helix	219	1
β-strand	220-225	6	15
β-strand	231-237	7	15
β-strand	240-244	5	15
β-strand	254-257	4	15
α-helix	258-260	3
β-strand	261-266	6	16
β-strand	271-275	5	16
α-helix	281-282	2
β-strand	283-285	3	16
β-strand	286	1	15
α-helix	290-310	21

Chain F: 11 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	22-27	6	17
β-strand	32-37	6	17
β-strand	42	1	18
α-helix	43-54	12
β-strand	62-68	7	17
β-strand	71-74	4	17
β-strand	80	1	18
β-strand	92-98	7	17
α-helix	105-108	4
α-helix	112-127	16
α-helix	135-150	16
α-helix	171-174	4
α-helix	181-192	12
α-helix	193-195	3
α-helix	200-211	12
β-strand	220-225	6	19
β-strand	231-236	6	19
β-strand	240-244	5	19
β-strand	254-257	4	19
α-helix	258-260	3
β-strand	261-267	7	19
β-strand	270-275	6	19
α-helix	281-282	2
β-strand	283-286	4	19
α-helix	290-310	21

Chain G: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	1481-1484	4	3

Chain H: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	1500-1503	4	6

2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Merlin	A, B, C, D, E, F	protein	301	Mus musculus	P46662 (AlphaFold model)
Protein VPRBP	G, H	protein	96	Homo sapiens	Q9Y4B6 (AlphaFold model)
Protein VPRBP	I	protein	7	Homo sapiens
Protein VPRBP	J	protein	8	Homo sapiens
Protein VPRBP	K	protein	6	Homo sapiens

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>3WA0_1 Merlin (chains A, B, C, D, E, F)
GPLGSPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA
WLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKVYC
PPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYA
EHRGRARDEAEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPK
ISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKA
D

Sequence of entity 2 (G, H), FASTA

>3WA0_2 Protein VPRBP (chains G, H)
GPLGSYDDDTDDLDELDTDQLLEAELEEDDNNENAGEDGDNDFSPSDEELANLLEEGEDG
EDEDSDADEEVELILGDTDSSDNSDLEDDIILSLNE

Sequence of entity 3 (I), FASTA

>3WA0_3 Protein VPRBP (chains I)
XXXXXXX

Sequence of entity 4 (J), FASTA

>3WA0_4 Protein VPRBP (chains J)
XXXXXXXX

Sequence of entity 5 (K), FASTA

>3WA0_5 Protein VPRBP (chains K)
XXXXXX

Primary citation

Structural basis of DDB1-and-Cullin 4-associated Factor 1 (DCAF1) recognition by merlin/NF2 and its implication in tumorigenesis by CD44-mediated inhibition of merlin suppression of DCAF1 function. Mori, T., Gotoh, S., Shirakawa, M. et al. Genes Cells (2014) 19:603-619. DOI 10.1111/gtc.12161 · PubMed

Other PDB entries of the same protein (UniProt P46662 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ZRK 2.32 Å, Merlin-FERM and Lats1 complex
4P7I 2.6 Å, Crystal structure of the Merlin FERM/DCAF1 complex
1ISN 2.9 Å, Crystal structure of merlin FERM domain

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