PDBsum entry 2bkd

Nuclear protein

PDB id: 2bkd

Contents

Protein chain

134 a.a. *

* Residue conservation analysis

PDB id:

2bkd

Name:

Nuclear protein

Title:

Structure of the n-terminal domain of fragile x mental retardation protein

Structure:

Fragile x messenger ribonucleoprotein 1. Chain: n. Fragment: residues 1-134. Synonym: fragile x messenger ribonucleoprotein,fmrp,protein fmr-1. Engineered: yes

Source:

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

NMR struc:

20 models

Authors:

A.Ramos,D.Hollingworth,S.Adinolfi,M.Castets,G.Kelly,T.A.Frenkiel, B.Bardoni,A.Pastore

Key ref:

A.Ramos et al. (2006). The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction. Structure, 14, 21-31. PubMed id: 16407062 DOI: 10.1016/j.str.2005.09.018

Date:

15-Feb-05 Release date: 18-Jan-06

Protein chain

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

Seq: 632 a.a.

Struc: 134 a.a.

DOI no: 10.1016/j.str.2005.09.018

Structure 14:21-31 (2006)

PubMed id: 16407062

The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction.

A.Ramos, D.Hollingworth, S.Adinolfi, M.Castets, G.Kelly, T.A.Frenkiel, B.Bardoni, A.Pastore.

ABSTRACT

FMRP, whose lack of expression causes the X-linked fragile X syndrome, is a modular RNA binding protein thought to be involved in posttranslational regulation. We have solved the structure in solution of the N-terminal domain of FMRP (NDF), a functionally important region involved in multiple interactions. The structure consists of a composite fold comprising two repeats of a Tudor motif followed by a short alpha helix. The interactions between the three structural elements are essential for the stability of the NDF fold. Although structurally similar, the two repeats have different dynamic and functional properties. The second, more flexible repeat is responsible for interacting both with methylated lysine and with 82-FIP, one of the FMRP nuclear partners. NDF contains a 3D nucleolar localization signal, since destabilization of its fold leads to altered nucleolar localization of FMRP. We suggest that the NDF composite fold determines an allosteric mechanism that regulates the FMRP functions.

Selected figure(s)

Figure 6.
Figure 6. Mapping the Interaction Surface of 82-FIP onto the NDF Structure
(A) Exposed hydrophobic patches (green) are shown on two surface representations of the NDF structure (white) that differ by a 180° rotation around the y axis. The orientation of the NDF structure on the left is the same as that in the right panel of Figure 2B.
(B) Residues involved in the interaction with 82-FIP156. The side chains of the residues that lead to marked (10, 13, 32, 64, 66, 67, 68, 70, 72-75, 79, 81-89, 91-95, 98, 101, 105, 107-110, 113) and minor (9, 14-16, 33, 69, 71, 80, 102) variations of the peak intensities in the HSQC are displayed in dark blue and light blue, respectively.
(C) Same as in (B), but in a ribbon representation showing explicitly the side chains of the residues affected.

The above figure is reprinted by permission from Cell Press: Structure (2006, 14, 21-31) copyright 2006.

Figure was selected by an automated process.