2g4b
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(New page: 200px<br /> <applet load="2g4b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g4b, resolution 2.5Å" /> '''Structure of U2AF65 ...)
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Revision as of 20:08, 12 November 2007
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Structure of U2AF65 variant with polyuridine tract
Overview
The essential pre-mRNA splicing factor, U2AF(65), guides the early stages, of splice site choice by recognizing a polypyrimidine (Py) tract consensus, sequence near the 3' splice site. Since Py tracts are relatively poorly, conserved in higher eukaryotes, U2AF(65) is faced with the problem of, specifying uridine-rich sequences, yet tolerating a variety of nucleotide, substitutions found in natural Py tracts. To better understand these, apparently contradictory RNA binding characteristics, the X-ray structure, of the U2AF(65) RNA binding domain bound to a Py tract composed of seven, uridines has been determined at 2.5 A resolution. Specific hydrogen bonds, between U2AF(65) and the uracil bases provide an explanation for, polyuridine recognition. Flexible side chains and bound water molecules, form the majority of the base contacts and potentially could rearrange, when the U2AF(65) structure adapts to different Py tract sequences. The, energetic importance of conserved residues for Py tract binding is, established by analysis of site-directed mutant U2AF(65) proteins using, surface plasmon resonance.
About this Structure
2G4B is a Single protein structure of sequence from Homo sapiens with DIO as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65., Sickmier EA, Frato KE, Shen H, Paranawithana SR, Green MR, Kielkopf CL, Mol Cell. 2006 Jul 7;23(1):49-59. PMID:16818232
Page seeded by OCA on Mon Nov 12 22:14:35 2007
