2wzo

From Proteopedia

(Difference between revisions)

Revision as of 19:06, 24 January 2018

The structure of the FYR domain

Structural highlights

2wzo is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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 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

↑ Tompkins VS, Hagen J, Frazier AA, Lushnikova T, Fitzgerald MP, di Tommaso A, Ladeveze V, Domann FE, Eischen CM, Quelle DE. A novel nuclear interactor of ARF and MDM2 (NIAM) that maintains chromosomal stability. J Biol Chem. 2007 Jan 12;282(2):1322-33. Epub 2006 Nov 16. PMID:17110379 doi:http://dx.doi.org/10.1074/jbc.M609612200
↑ Garcia-Alai MM, Allen MD, Joerger AC, Bycroft M. The structure of the FYR domain of transforming growth factor beta regulator 1 (TBRG1). Protein Sci. 2010 Apr 21. PMID:20506279 doi:10.1002/pro.404

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wzo"

@@ Line 1: / Line 1: @@
-==THE STRUCTURE OF THE FYR DOMAIN==
+==The structure of the FYR domain==
 <StructureSection load='2wzo' size='340' side='right' caption='[[2wzo]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
@@ Line 13: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wz/2wzo_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wz/2wzo_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2wzo

From Proteopedia

Revision as of 19:06, 24 January 2018

The structure of the FYR domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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