Structural insights into the recruitment of SMRT by the co-repressor SHARP under phosphorylative regulation. Determined by solution NMR. Released 4 Dec 2013.
Explore 2RT5 in 3D Show helices and sheets RCSB PDB PDBe
2RT5 contains 10 α-helices and 9 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 3498-3501 | 4 | |
| β-strand | 3507-3515 | 9 | 1 |
| β-strand | 3518-3529 | 12 | 1 |
| α-helix | 3531-3537 | 7 | |
| α-helix | 3545-3546 | 2 | |
| β-strand | 3547-3548 | 2 | 1 |
| β-strand | 3551-3552 | 2 | 1 |
| α-helix | 3557-3567 | 11 | |
| β-strand | 3570 | 1 | 1 |
| β-strand | 3573-3580 | 8 | 1 |
| α-helix | 3585-3595 | 11 | |
| α-helix | 3596-3600 | 5 | |
| α-helix | 3601-3606 | 6 | |
| β-strand | 3610-3614 | 5 | 1 |
| α-helix | 3615-3616 | 2 | |
| β-strand | 3624-3629 | 6 | 1 |
| α-helix | 3633-3642 | 10 | |
| α-helix | 3644-3650 | 7 | |
| β-strand | 3657-3663 | 7 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Msx2-interacting protein | A | protein | 169 | Homo sapiens | Q96T58 |
| peptide from Silencing mediator of retinoic acid and thyroid hormone receptor | B | protein | 8 | Homo sapiens | Q9Y618 (AlphaFold model) |
>2RT5_1 Msx2-interacting protein (chains A) VDMVQLLKKYPIVWQGLLALKNDTAAVQLHFVSGNNVLAHRSLPLSEGGPPLRIAQRMRL EATQLEGVARRMTVETDYCLLLALPCGRDQEDVVSQTESLKAAFITYLQAKQAAGIINVP NPGSNQPAYVLQIFPPCEFSESHLSRLAPDLLASISNISPHLMIVIASV
>2RT5_2 peptide from Silencing mediator of retinoic acid and thyroid hormone receptor (chains B) YETLSDSE
Structural insights into the recruitment of SMRT by the corepressor SHARP under phosphorylative regulation. Mikami, S., Kanaba, T., Takizawa, N. et al. Structure (2014) 22:35-46. DOI 10.1016/j.str.2013.10.007 · PubMed
Other PDB entries of the same protein (UniProt Q96T58), best resolution first:
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