Proteomics

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Integrative structure determination of an 85-kilodalton PTBP1-IRES complex in solution reveals a strong compaction with pronounced conformational flexibility

ABSTRACT: Cross-linking of isotope-labelled RNA coupled with mass spectrometry (CLIR-MS) was used to study the interaction between the four RNA recognition motifs (RRMs) of the protein PTBP1 with the internal ribosome entry site (IRES) of encephalomyocarditis virus (EMCV). These results are a reanalysis of PXD005566, with a broader parameter set.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Christopher Sarnowski  

LAB HEAD: Alexander Leitner

PROVIDER: PXD034894 | Pride | 2023-10-24

REPOSITORIES: Pride

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RNA-binding proteins (RBPs) are crucial regulators of gene expression, often composed of defined domains interspersed with flexible, intrinsically disordered regions. Determining the structure of ribonucleoprotein (RNP) complexes involving such RBPs necessitates integrative structural modeling due to their lack of a single stable state. In this study, we integrate magnetic resonance, mass spectrometry, and small-angle scattering data to determine the solution structure of the polypyrimidine-trac  ...[more]

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