Structural highlights
Function
[TXN4B_HUMAN] Essential role in pre-mRNA splicing. Required in cell cycle progression for S/G(2) transition.[1]
Publication Abstract from PubMed
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 A 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 beta-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.
High-resolution crystal structure of human Dim2/TXNL4B.,Jin T, Guo F, Wang Y, Zhang Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):223-7. doi:, 10.1107/S1744309113000973. Epub 2013 Feb 22. PMID:23519793[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sun X, Zhang H, Wang D, Ma D, Shen Y, Shang Y. DLP, a novel Dim1 family protein implicated in pre-mRNA splicing and cell cycle progression. J Biol Chem. 2004 Jul 30;279(31):32839-47. Epub 2004 May 25. PMID:15161931 doi:10.1074/jbc.M402522200
- ↑ Jin T, Guo F, Wang Y, Zhang Y. High-resolution crystal structure of human Dim2/TXNL4B. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):223-7. doi:, 10.1107/S1744309113000973. Epub 2013 Feb 22. PMID:23519793 doi:10.1107/S1744309113000973
