2wzo
From Proteopedia
The structure of the FYR domain
Structural highlights
Function[TBRG1_HUMAN] Acts as a growth inhibitor. Can activate p53/TP53, causes G1 arrest and collaborates with CDKN2A to restrict proliferation, but does not require either protein to inhibit DNA synthesis. Redistributes CDKN2A into the nucleoplasm. Involved in maintaining chromosomal stability.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMany 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 TBRG1 (transforming growth factor beta regulator 1)/ NIAM (Nuclear interactor of ARF and MDM2), 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. The structure of the FYR domain of transforming growth factor beta regulator 1 (TBRG1).,Garcia-Alai MM, Allen MD, Joerger AC, Bycroft M Protein Sci. 2010 Apr 21. PMID:20506279[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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