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New page: left|200px<br /> <applet load="1cok" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cok" /> '''STRUCTURE OF THE C-TERMINAL DOMAIN OF P73''...
 
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[[Image:1cok.gif|left|200px]]<br />
[[Image:1cok.gif|left|200px]]<br /><applet load="1cok" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1cok" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1cok" />
caption="1cok" />
'''STRUCTURE OF THE C-TERMINAL DOMAIN OF P73'''<br />
'''STRUCTURE OF THE C-TERMINAL DOMAIN OF P73'''<br />


==Overview==
==Overview==
p73 and p63 are two recently cloned genes with homology to the tumor, suppressor p53, whose protein product is a key transcriptional regulator, of genes involved in cell cycle arrest and apoptosis. While all three, proteins share conserved transcriptional activation, DNA-binding and, oligomerization domains, p73 and p63 have an additional conserved, C-terminal region. We have determined the three-dimensional solution, structure of this conserved C-terminal domain of human p73. The structure, reveals a small five-helix bundle with striking similarity to the SAM, (sterile alpha motif) domains of two ephrin receptor tyrosine kinases. The, SAM domain is a putative protein-protein interaction domain found in a, variety of cytoplasmic signaling proteins and has been shown to form both, homo- and hetero-oligomers. However, the SAM-like C-terminal domains of, p73 and p63 are monomeric and do not interact with one another, suggesting, that this domain may interact with additional, as yet uncharacterized, proteins in a signaling and/or regulatory role.
p73 and p63 are two recently cloned genes with homology to the tumor suppressor p53, whose protein product is a key transcriptional regulator of genes involved in cell cycle arrest and apoptosis. While all three proteins share conserved transcriptional activation, DNA-binding and oligomerization domains, p73 and p63 have an additional conserved C-terminal region. We have determined the three-dimensional solution structure of this conserved C-terminal domain of human p73. The structure reveals a small five-helix bundle with striking similarity to the SAM (sterile alpha motif) domains of two ephrin receptor tyrosine kinases. The SAM domain is a putative protein-protein interaction domain found in a variety of cytoplasmic signaling proteins and has been shown to form both homo- and hetero-oligomers. However, the SAM-like C-terminal domains of p73 and p63 are monomeric and do not interact with one another, suggesting that this domain may interact with additional, as yet uncharacterized proteins in a signaling and/or regulatory role.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1COK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1COK OCA].  
1COK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COK OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Arrowsmith, C.H.]]
[[Category: Arrowsmith, C H.]]
[[Category: Ayed, A.]]
[[Category: Ayed, A.]]
[[Category: Chi, S.W.]]
[[Category: Chi, S W.]]
[[Category: gene regulation]]
[[Category: gene regulation]]
[[Category: p73 sam-like domain]]
[[Category: p73 sam-like domain]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:24:16 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:05 2008''