1hn3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hn3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HN3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1hn3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HN3 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hn3 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn3 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hn3 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn3 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Bothner, B | [[Category: Bothner, B]] | ||
[[Category: DiGiammarino, E L | [[Category: DiGiammarino, E L]] | ||
[[Category: Filippov, I | [[Category: Filippov, I]] | ||
[[Category: Kriwacki, R W | [[Category: Kriwacki, R W]] | ||
[[Category: Weber, J D | [[Category: Weber, J D]] | ||
[[Category: Antitumor protein]] | [[Category: Antitumor protein]] | ||
[[Category: Arf]] | [[Category: Arf]] | ||
Revision as of 00:41, 23 December 2014
SOLUTION STRUCTURE OF THE N-TERMINAL 37 AMINO ACIDS OF THE MOUSE ARF TUMOR SUPPRESSOR PROTEINSOLUTION STRUCTURE OF THE N-TERMINAL 37 AMINO ACIDS OF THE MOUSE ARF TUMOR SUPPRESSOR PROTEIN
Structural highlights
Publication Abstract from PubMedArf is a tumor suppressor that regulates p53 function and is a frequent target for loss in human cancers. Through two novel mechanisms, Arf inhibits the oncoprotein Hdm2, a negative regulator of p53. (1) Arf inhibits the E3 ubiquitin ligase activity of Hdm2 that leads to p53 degradation, and (2) Arf sequesters Hdm2 within nucleoli. These activities of Arf promote p53-mediated cell cycle arrest and apoptosis. Fundamental to these processes are interactions between Arf and Hdm2. Here we show that a peptide containing the 37 N-terminal amino acids of mouse Arf (mArfN37) localizes to nucleoli, sequesters Hdm2 within nucleoli, and causes cell cycle arrest. Circular dichroism and NMR spectroscopy show that mArfN37 is largely unstructured under aqueous conditions; however, the peptide adopts two alpha-helices (helix 1, residues 4-14; and helix 2, residues 20-29) in 2,2,2-trifluoroethanol (TFE). Each helix contains an amino acid motif that is repeated twice in mArfN37, once in each helix. The two helices, however, do not interact but are connected by an apparently flexible linker. The repeated motif contains Arg residues spaced by a hydrophobic segment that may be involved in Hdm2 recognition and binding. The RRPR nucleolar localization signal, contained within residues 31-34, appears to be disordered under all conditions. The identification of two Arf structural modules suggests that short peptides containing the repeated motif may function as Arf mimics and may allow the design of small molecule Arf mimics in the future. Solution structure of the p53 regulatory domain of the p19Arf tumor suppressor protein.,DiGiammarino EL, Filippov I, Weber JD, Bothner B, Kriwacki RW Biochemistry. 2001 Feb 27;40(8):2379-86. PMID:11327858[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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