2RT5: Msx2-interacting protein

Structural insights into the recruitment of SMRT by the co-repressor SHARP under phosphorylative regulation. Determined by solution NMR. Released 4 Dec 2013.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,370
Mol. weight
19.57 kDa
Released
4 Dec 2013

Explore 2RT5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 10 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix3498-35014
β-strand3507-351591
β-strand3518-3529121
α-helix3531-35377
α-helix3545-35462
β-strand3547-354821
β-strand3551-355221
α-helix3557-356711
β-strand357011
β-strand3573-358081
α-helix3585-359511
α-helix3596-36005
α-helix3601-36066
β-strand3610-361451
α-helix3615-36162
β-strand3624-362961
α-helix3633-364210
α-helix3644-36507
β-strand3657-366371

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Msx2-interacting proteinAprotein169Homo sapiensQ96T58
peptide from Silencing mediator of retinoic acid and thyroid hormone receptorBprotein8Homo sapiensQ9Y618 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2RT5_1 Msx2-interacting protein (chains A)
VDMVQLLKKYPIVWQGLLALKNDTAAVQLHFVSGNNVLAHRSLPLSEGGPPLRIAQRMRL
EATQLEGVARRMTVETDYCLLLALPCGRDQEDVVSQTESLKAAFITYLQAKQAAGIINVP
NPGSNQPAYVLQIFPPCEFSESHLSRLAPDLLASISNISPHLMIVIASV
Sequence of entity 2 (B), FASTA
>2RT5_2 peptide from Silencing mediator of retinoic acid and thyroid hormone receptor (chains B)
YETLSDSE

Primary citation

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:

Browse structure collections

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