4OZ0
Crystal structure of human CAPERalpha U2AF homology motif (apo-state)
Summary for 4OZ0
| Entry DOI | 10.2210/pdb4oz0/pdb |
| Descriptor | RNA-binding protein 39, CHLORIDE ION (3 entities in total) |
| Functional Keywords | u2af homology motif, uhm, protein-peptide complex, pre-mrna splicing factor, transcription |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 25356.12 |
| Authors | Loerch, S.,Kielkopf, C.L. (deposition date: 2014-02-13, release date: 2014-05-14, Last modification date: 2023-09-27) |
| Primary citation | Loerch, S.,Maucuer, A.,Manceau, V.,Green, M.R.,Kielkopf, C.L. Cancer-relevant splicing factor CAPER alpha engages the essential splicing factor SF3b155 in a specific ternary complex. J.Biol.Chem., 289:17325-17337, 2014 Cited by PubMed Abstract: U2AF homology motifs (UHMs) mediate protein-protein interactions with U2AF ligand motifs (ULMs) of pre-mRNA splicing factors. The UHM-containing alternative splicing factor CAPERα regulates splicing of tumor-promoting VEGF isoforms, yet the molecular target of the CAPERα UHM is unknown. Here we present structures of the CAPERα UHM bound to a representative SF3b155 ULM at 1.7 Å resolution and, for comparison, in the absence of ligand at 2.2 Å resolution. The prototypical UHM/ULM interactions authenticate CAPERα as a bona fide member of the UHM family of proteins. We identify SF3b155 as the relevant ULM-containing partner of full-length CAPERα in human cell extracts. Isothermal titration calorimetry comparisons of the purified CAPERα UHM binding known ULM-containing proteins demonstrate that high affinity interactions depend on the presence of an intact, intrinsically unstructured SF3b155 domain containing seven ULM-like motifs. The interplay among bound CAPERα molecules gives rise to the appearance of two high affinity sites in the SF3b155 ULM-containing domain. In conjunction with the previously identified, UHM/ULM-mediated complexes of U2AF(65) and SPF45 with SF3b155, this work demonstrates the capacity of SF3b155 to offer a platform for coordinated recruitment of UHM-containing splicing factors. PubMed: 24795046DOI: 10.1074/jbc.M114.558825 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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