8CIT: The FERM domain of human moesin mutant L281R

The FERM domain of human moesin mutant L281R. Determined by X-ray diffraction at 2.54 Å resolution. Released 1 Mar 2023.

Method: X-ray diffraction
Resolution: 2.54 Å
Organism: Homo sapiens
Chains: 3
Atoms: 8,259
Mol. weight: 123.56 kDa
Released: 1 Mar 2023

Explore 8CIT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8CIT contains 44 α-helices and 48 β-strands across 3 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: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	1
β-strand	15-20	6	1
β-strand	25	1	2
α-helix	26-37	12
α-helix	42-44	3
β-strand	45-50	6	1
β-strand	51	1	3
β-strand	56-58	3	1
α-helix	59-60	2
β-strand	64	1	2
α-helix	65-67	3
β-strand	70	1	3
β-strand	76-82	7	1
α-helix	89-92	4
α-helix	96-111	16
α-helix	119-134	16
α-helix	155-160	6
α-helix	165-178	14
α-helix	184-195	12
β-strand	204-209	6	4
β-strand	215-221	7	4
β-strand	224-229	6	4
β-strand	236-241	6	4
α-helix	242-244	3
β-strand	245-251	7	4
β-strand	254-259	6	4
α-helix	265-266	2
β-strand	267-270	4	4
α-helix	274-295	22
α-helix	297-299	3
α-helix	300-339	40

Chain B: 14 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	5
β-strand	15-20	6	5
β-strand	25	1	6
α-helix	26-37	12
α-helix	42-44	3
β-strand	45-50	6	5
β-strand	51	1	7
β-strand	56-58	3	5
α-helix	59-60	2
β-strand	64	1	6
α-helix	65-67	3
β-strand	70	1	7
β-strand	76-82	7	5
α-helix	89-92	4
α-helix	96-111	16
α-helix	119-134	16
α-helix	155-160	6
α-helix	165-178	14
α-helix	184-195	12
β-strand	204-209	6	8
β-strand	215-221	7	8
β-strand	224-229	6	8
β-strand	236-241	6	8
β-strand	245-250	6	8
β-strand	254-259	6	8
α-helix	265-266	2
β-strand	267-270	4	8
α-helix	274-295	22
α-helix	297-299	3
α-helix	300-342	43

Chain C: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	9
β-strand	15-20	6	9
β-strand	25	1	10
α-helix	26-37	12
α-helix	42-44	3
β-strand	45-50	6	9
β-strand	51	1	11
β-strand	56-58	3	9
α-helix	59-60	2
β-strand	64	1	10
α-helix	65-67	3
β-strand	70	1	11
β-strand	76-82	7	9
α-helix	89-92	4
α-helix	96-111	16
α-helix	119-134	16
α-helix	155-160	6
α-helix	165-178	14
α-helix	184-195	12
β-strand	204-209	6	12
β-strand	215-221	7	12
β-strand	224-229	6	12
β-strand	236-241	6	12
α-helix	242-244	3
β-strand	245-250	6	12
β-strand	254-259	6	12
α-helix	265-266	2
β-strand	267-270	4	12
α-helix	274-294	21
α-helix	297-299	3
α-helix	300-326	27

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Moesin	A, B, C	protein	347	Homo sapiens	P26038 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>8CIT_1 Moesin (chains A, B, C)
SMPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWL
KLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPP
ETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEH
RGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIG
FPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRIRALCMGNHELYMRRRKPDT
IEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEE

Primary citation

Discovery of FERM domain protein-protein interaction inhibitors for MSN and CD44 as a potential therapeutic approach for Alzheimer's disease. Du, Y., Bradshaw, W.J., Leisner, T.M. et al. J Biol Chem (2023) 299:105382-105382. DOI 10.1016/j.jbc.2023.105382 · PubMed

Other PDB entries of the same protein (UniProt P26038 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8CIS 1.52 Å, The FERM domain of human moesin with two bound peptides identified by phage display
6TXQ 1.73 Å, The high resolution structure of the FERM domain and helical linker of human moesin
8XZ5 1.8 Å, SARS-CoV-2 S and moesin complex structure
8CIR 1.85 Å, The FERM domain of human moesin with a bound peptide identified by phage display
1EF1 1.9 Å, Crystal structure of the moesin ferm domain/tail domain complex
6TXS 2.2 Å, The structure of the FERM domain and helical linker of human moesin bound to a CD44…
8CIU 2.39 Å, The FERM domain of human moesin mutant H288A
1E5W 2.7 Å, Structure of isolated FERM domain and first long helix of moesin
1SGH 3.5 Å, Moesin FERM domain bound to EBP50 C-terminal peptide

Browse structure collections

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