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7PU5

Structure of SFPQ-NONO complex

Summary for 7PU5
Entry DOI10.2210/pdb7pu5/pdb
DescriptorNon-POU domain-containing octamer-binding protein, Splicing factor, proline- and glutamine-rich, MAGNESIUM ION (3 entities in total)
Functional Keywordsdbhs, paraspeckle, nops, rrm, nuclear protein
Biological sourceHomo sapiens (Human)
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Total number of polymer chains12
Total formula weight358635.73
Authors
Fribourg, S. (deposition date: 2021-09-28, release date: 2022-03-16, Last modification date: 2024-01-31)
Primary citationSchell, B.,Legrand, P.,Fribourg, S.
Crystal structure of SFPQ-NONO heterodimer.
Biochimie, 198:1-7, 2022
Cited by
PubMed Abstract: The Drosophila behavior/human splicing (DBHS) protein family is composed of the three members SFPQ, NONO and PSPC1. These proteins share a strong sequence and structural homology within the core-structured domains forming obligate homo- and heterodimers. This feature may lead to the simultaneous existence of six different dimeric complexes that sustain their function in many cellular processes such as pre-mRNA splicing, innate immunity, transcriptional regulation. In order to perform a complete structural analysis of all possible DBHS dimers, we have solved the crystal structure of the missing DBHS heterodimer SFPQ-NONO at 3.0 Å resolution. We identify subtle changes in amino acid composition and local secondary structure of the NOPS region orientation that may modulate affinity between complexes. Interestingly this area is found mutated in aggressive skin cancers and adenocarcinomas.
PubMed: 35245601
DOI: 10.1016/j.biochi.2022.02.011
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.999 Å)
Structure validation

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数据于2025-12-17公开中

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