4IN0
Crystal Structure of human splicing factor dim2/TXNL4B
Summary for 4IN0
Entry DOI | 10.2210/pdb4in0/pdb |
Related PRD ID | PRD_900003 |
Descriptor | Thioredoxin-like protein 4B, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose (3 entities in total) |
Functional Keywords | pre-mrna splicing, splicing |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus : Q9NX01 |
Total number of polymer chains | 2 |
Total formula weight | 34149.13 |
Authors | Jin, T.C.,Guo, F.,Zhang, Y.Z. (deposition date: 2013-01-03, release date: 2013-03-13, Last modification date: 2023-09-20) |
Primary citation | Jin, T.,Guo, F.,Wang, Y.,Zhang, Y. High-resolution crystal structure of human Dim2/TXNL4B. Acta Crystallogr.,Sect.F, 69:223-227, 2013 Cited by PubMed Abstract: TXNL4A (thioredoxin-like 4A) is an essential protein conserved from yeast to humans and is a component of the pre-mRNA splicing machinery. TXNL4B was identified as a TXNL4-family protein that also interacts with Prp6, an integral component of the U4/U6·U5 tri-snRNP complex, and has been shown to function in pre-mRNA splicing. A crystal structure of TXNL4B was determined at 1.33 Å resolution and refined to an Rwork of 0.13 and an Rfree of 0.18 with one native dimer in the asymmetric unit. Residues 1-33 of TXNL4B have previously been reported to be responsible for its interaction with Prp6. However, this region extends to the β-sheet core of the thioredoxin-fold structure of TXNL4B. This suggests that the interpretation of the previously reported GST pull-down results without considering the structure and stability of TXNL4B is debatable. PubMed: 23519793DOI: 10.1107/S1744309113000973 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.327 Å) |
Structure validation
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