1SYX

The crystal structure of a binary U5 snRNP complex

Summary for 1SYX

• Entry DOI: 10.2210/pdb1syx/pdb
• Related: 1GYF 1QGV
• Descriptor: Spliceosomal U5 snRNP-specific 15 kDa protein, CD2 antigen cytoplasmic tail-binding protein 2 (3 entities in total)
• Functional Keywords: gyf-domain; thioredoxin-like; spliceosomal proteins, translation-immune system complex, translation/immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 6
• Total formula weight: 80049.07

Authors

Nielsen, T.K.,Liu, S.,Luhrmann, R.,Ficner, R. (deposition date: 2004-04-02, release date: 2005-10-18, Last modification date: 2023-08-23)

Primary citation

Nielsen, T.K.,Liu, S.,Luhrmann, R.,Ficner, R.
Structural basis for the bifunctionality of the U5 snRNP 52K protein (CD2BP2).
J.Mol.Biol., 369:902-908, 2007

PubMed Abstract: The bifunctional protein U5-52K is associated with the spliceosomal 20 S U5 snRNP, and it also plays a role in immune response as CD2 receptor binding protein 2 (CD2BP2). U5-52K binds to the CD2 receptor via its GYF-domain specifically recognizing a proline-rich motif on the cytoplasmic surface of the receptor. The GYF-domain is also mediating the interaction of the proteins U5-52K and U5-15K within the spliceosomal U5 snRNP. Here we report the crystal structure of the complex of GYF-domain and U5-15K protein revealing the structural basis for the bifunctionality of the U5-52K protein. The complex structure unveils novel interaction sites on both proteins, as neither the polyproline-binding site of the GYF-domain nor the common ligand-binding cleft of thioredoxin-like proteins, to which U5-15K belongs, are involved in the interaction of U5-15K and U5-52K.

PubMed: 17467737
DOI: 10.1016/j.jmb.2007.03.077

Experimental method

X-RAY DIFFRACTION (2.345 Å)