The FERM domain of human moesin with a bound peptide identified by phage display. Determined by X-ray diffraction at 1.85 Å resolution. Released 1 Mar 2023.
Explore 8CIR in 3D Show helices and sheets RCSB PDB PDBe
8CIR contains 33 α-helices and 32 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.
| 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 | 238-241 | 4 | 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 | 300-333 | 34 |
| 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 | 238-241 | 4 | 8 |
| α-helix | 242-244 | 3 | |
| β-strand | 245-251 | 7 | 8 |
| β-strand | 254-259 | 6 | 8 |
| α-helix | 265-266 | 2 | |
| β-strand | 267-270 | 4 | 8 |
| α-helix | 274-294 | 21 | |
| α-helix | 297-299 | 3 | |
| α-helix | 300-333 | 34 | |
| α-helix | 337-343 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-15 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Moesin | A, B | protein | 347 | Homo sapiens | P26038 (AlphaFold model) |
| C3P | C, D | protein | 16 | synthetic construct |
>8CIR_1 Moesin (chains A, B) SMPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWL KLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPP ETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEH RGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIG FPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDT IEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEE
>8CIR_2 C3P (chains C, D) EDGGSWKYPDAFELSG
| ID | Name | Formula | Copies |
|---|---|---|---|
| B3P | 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-pr… | C11 H26 N2 O6 | 2 |
Water and common crystallization additives (BR, EDO) are not listed.
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:
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