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1SJR

NMR Structure of RRM2 from Human Polypyrimidine Tract Binding Protein Isoform 1 (PTB1)

Summary for 1SJR
Entry DOI10.2210/pdb1sjr/pdb
Related1sjq
NMR InformationBMRB: 6177
DescriptorPolypyrimidine tract-binding protein 1 (1 entity in total)
Functional Keywordsextended babbab motif, rna binding protein
Biological sourceHomo sapiens (human)
Cellular locationNucleus: P26599
Total number of polymer chains1
Total formula weight17758.07
Authors
Simpson, P.J.,Monie, T.P.,Szendroi, A.,Davydova, N.,Tyzack, J.K.,Conte, M.R.,Read, C.M.,Cary, P.D.,Svergun, D.I.,Konarev, P.V.,Petoukhov, M.V.,Curry, S.,Matthews, S.J. (deposition date: 2004-03-04, release date: 2004-09-14, Last modification date: 2024-05-22)
Primary citationSimpson, P.J.,Monie, T.P.,Szendroi, A.,Davydova, N.,Tyzack, J.K.,Conte, M.R.,Read, C.M.,Cary, P.D.,Svergun, D.I.,Konarev, P.V.,Curry, S.,Matthews, S.J.
Structure and RNA Interactions of the N-Terminal RRM Domains of PTB
Structure, 12:1631-1643, 2004
Cited by
PubMed Abstract: The polypyrimidine tract binding protein (PTB) is an important regulator of alternative splicing that also affects mRNA localization, stabilization, polyadenylation, and translation. NMR structural analysis of the N-terminal half of PTB (residues 55-301) shows a canonical structure for RRM1 but reveals novel extensions to the beta strands and C terminus of RRM2 that significantly modify the beta sheet RNA binding surface. Although PTB contains four RNA recognition motifs (RRMs), it is widely held that only RRMs 3 and 4 are involved in RNA binding and that RRM2 mediates homodimerization. However, we show here not only that the RRMs 1 and 2 contribute substantially to RNA binding but also that full-length PTB is monomeric, with an elongated structure determined by X-ray solution scattering that is consistent with a linear arrangement of the constituent RRMs. These new insights into the structure and RNA binding properties of PTB suggest revised models of its mechanism of action.
PubMed: 15341728
DOI: 10.1016/j.str.2004.07.008
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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