PDBsum entry 4qw2

Translation

PDB id: 4qw2

Contents

Protein chains

198 a.a.

Ligands

EDO

Metals

_PB

Waters ×11

PDB id:

4qw2

Name:

Translation

Title:

Fmrp n-terminal domain (r138q)

Structure:

Fragile x mental retardation protein 1. Chain: a, b. Fragment: n-terminal domain (unp residues 1-213). Synonym: fmrp, protein fmr-1. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: fmr1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.99Å R-factor: 0.229 R-free: 0.283

Authors:

L.K.Myrick,H.Hashimoto,X.Cheng,S.T.Warren

Key ref:

L.K.Myrick et al. (2015). Human FMRP contains an integral tandem Agenet (Tudor) and KH motif in the amino terminal domain. Hum Mol Genet, 24, 1733-1740. PubMed id: 25416280 DOI: 10.1093/hmg/ddu586

Date:

16-Jul-14 Release date: 03-Dec-14

Protein chains

Q06787  (FMR1_HUMAN) -  Fragile X messenger ribonucleoprotein 1 from Homo sapiens

Seq: 632 a.a.

Struc: 198 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1093/hmg/ddu586

Hum Mol Genet 24:1733-1740 (2015)

PubMed id: 25416280

Human FMRP contains an integral tandem Agenet (Tudor) and KH motif in the amino terminal domain.

L.K.Myrick, H.Hashimoto, X.Cheng, S.T.Warren.

ABSTRACT

Fragile X syndrome, a common cause of intellectual disability and autism, is due to mutational silencing of the FMR1 gene leading to the absence of its gene product, fragile X mental retardation protein (FMRP). FMRP is a selective RNA binding protein owing to two central K-homology domains and a C-terminal arginine-glycine-glycine (RGG) box. However, several properties of the FMRP amino terminus are unresolved. It has been documented for over a decade that the amino terminus has the ability to bind RNA despite having no recognizable functional motifs. Moreover, the amino terminus has recently been shown to bind chromatin and influence the DNA damage response as well as function in the presynaptic space, modulating action potential duration. We report here the amino terminal crystal structures of wild-type FMRP, and a mutant (R138Q) that disrupts the amino terminus function, containing an integral tandem Agenet and discover a novel KH motif.