2WZO

The structure of the FYR domain

Summary for 2WZO

• Entry DOI: 10.2210/pdb2wzo/pdb
• Descriptor: TRANSFORMING GROWTH FACTOR BETA REGULATOR 1, GLYCEROL (3 entities in total)
• Functional Keywords: nucleus, cell cycle, tumor suppressor
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus : Q3YBR2
• Total number of polymer chains: 1
• Total formula weight: 16140.42

Authors

Garcia-Alai, M.M.,Allen, M.D.,Joerger, A.C.,Bycroft, M. (deposition date: 2009-12-01, release date: 2010-05-05, Last modification date: 2024-05-08)

Primary citation

Garcia-Alai, M.M.,Allen, M.D.,Joerger, A.C.,Bycroft, M.
The Structure of the Fyr Domain of Transforming Growth Factor Beta Regulator 1 (Tbrg1)(Pna)
Protein Sci., 19:1432-, 2010

PubMed 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 alpha + beta 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 beta-sheet.

PubMed: 20506279
DOI: 10.1002/PRO.404

Experimental method

X-RAY DIFFRACTION (1.6 Å)