The structure of the FYR domain of transforming growth factor beta regulator 1

DOI: 10.1002/pro.404
PMID: 20506279

Authors: Maria Garcia-Alai (MRC Centre for Protein Engineering) , Mark D. Allen (MRC Centre for Protein Engineering) , Andreas C. Joerger (Centre for Protein Engineering, Medical Research Council) , Mark Bycroft (MRC Centre for Protein Engineering)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Protein Science , VOL 19 (7) , PAGES 1432-1438

State: Published (Approved)
Published: April 2010

Abstract: Many chromatin-associated proteins contain two sequence motifs rich in phenylalanine/tyrosine residues of unknown function. These so-called FYRN and FYRC motifs are also found in transforming growth factor beta regulator 1 (TBRG1)/nuclear interactor of ARF and MDM2 (NIAM), a growth inhibitory protein that also plays a role in maintaining chromosomal stability. We have solved the structure of a fragment of TBRG1, which encompasses both of these motifs. The FYRN and FYRC regions each form part of a single folded module (the FYR domain), which adopts a novel α + β fold. Proteins such as the histone H3K4 methyltransferases trithorax and mixed lineage leukemia (MLL), in which the FYRN and FYRC regions are separated by hundreds of amino acids, are expected to contain FYR domains with a large insertion between two of the strands of the β-sheet.

Journal Keywords: Calorimetry; Differential; Circular; Humans; Intracellular; Molecular; Nuclear; Protein; Secondary; Protein; Tertiary; Spectrometry; Fluorescence

Diamond Keywords: Leukaemia

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography

Added On: 26/01/2011 18:50

Documents:
Protein Science - 2010 - Garc a%E2%80%90Alai - The structure of the FYR domain of transforming growth factor beta regulator 1.pdf

Discipline Tags:

Non-Communicable Diseases Health & Wellbeing Cancer Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)