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1jmt
From Proteopedia
| 1jmt, resolution 2.20Å () | |||||||||
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| Ligands: | |||||||||
| Domains: | RRM_1 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
X-ray Structure of a Core U2AF65/U2AF35 Heterodimer
U2 auxiliary factor (U2AF) is an essential splicing factor that recognizes the 3' splice site and recruits the U2 snRNP to the branch point. The X-ray structure of the human core U2AF heterodimer, consisting of the U2AF35 central domain and a proline-rich region of U2AF65, has been determined at 2.2 A resolution. The structure reveals a novel protein-protein recognition strategy, in which an atypical RNA recognition motif (RRM) of U2AF35 and the U2AF65 polyproline segment interact via reciprocal "tongue-in-groove" tryptophan residues. Complementary biochemical experiments demonstrate that the core U2AF heterodimer binds RNA, and that the interacting tryptophan side chains are essential for U2AF dimerization. Atypical RRMs in other splicing factors may serve as protein-protein interaction motifs elsewhere during spliceosome assembly.
A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer., Kielkopf CL, Rodionova NA, Green MR, Burley SK, Cell. 2001 Sep 7;106(5):595-605. PMID:11551507
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1JMT is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Kielkopf CL, Rodionova NA, Green MR, Burley SK. A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer. Cell. 2001 Sep 7;106(5):595-605. PMID:11551507
Page seeded by OCA on Wed Feb 18 07:25:17 2009
