PDBsum entry 5o2v

RNA binding protein

PDB id: 5o2v

Contents

Protein chain

92 a.a.

PDB id:

5o2v

Name:

RNA binding protein

Title:

Nmr structure of tia-1 rrm1 domain

Structure:

Nucleolysin tia-1 isoform p40. Chain: a. Fragment: rrm1 domain, unp residues 1-92. Synonym: RNA-binding protein tia-1,t-cell-restricted intracellular antigen-1,tia-1,p40-tia-1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: tia1. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

20 models

Authors:

P.K.A.Jagtap

Key ref:

M.Sonntag et al. (2017). Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins. Angew Chem Int Ed Engl, 56, 9322-9325. PubMed id: 28636238 DOI: 10.1002/anie.201702904

Date:

22-May-17 Release date: 28-Jun-17

Protein chain

P31483  (TIA1_HUMAN) -  Cytotoxic granule associated RNA binding protein TIA1 from Homo sapiens

Seq: 386 a.a.

Struc: 92 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1002/anie.201702904

Angew Chem Int Ed Engl 56:9322-9325 (2017)

PubMed id: 28636238

Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins.

M.Sonntag, P.K.A.Jagtap, B.Simon, M.S.Appavou, A.Geerlof, R.Stehle, F.Gabel, J.Hennig, M.Sattler.

ABSTRACT

Multi-domain proteins play critical roles in fine-tuning essential processes in cellular signaling and gene regulation. Typically, multiple globular domains that are connected by flexible linkers undergo dynamic rearrangements upon binding to protein, DNA or RNA ligands. RNA binding proteins (RBPs) represent an important class of multi-domain proteins, which regulate gene expression by recognizing linear or structured RNA sequence motifs. Here, we employ segmental perdeuteration of the three RNA recognition motif (RRM) domains in the RBP TIA-1 using Sortase A mediated protein ligation. We show that domain-selective perdeuteration combined with contrast-matched small-angle neutron scattering (SANS), SAXS and computational modeling provides valuable information to precisely define relative domain arrangements. The approach is generally applicable to study conformational arrangements of individual domains in multi-domain proteins and changes induced by ligand binding.