1c26: Difference between revisions

Line 1:

[[Image:1c26.gif|left|200px]]<br />

[[Image:1c26.gif|left|200px]]<br /><applet load="1c26" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1c26" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1c26, resolution 1.7Å" />

'''CRYSTAL STRUCTURE OF P53 TETRAMERIZATION DOMAIN'''<br />

==Overview==

The p53 protein is a tetrameric transcription factor that plays a central, role in the prevention of neoplastic transformation. Oligomerization, appears to be essential for the tumor suppressing activity of p53 because, oligomerization-deficient p53 mutants cannot suppress the growth of, carcinoma cell lines. The crystal structure of the tetramerization domain, of p53 (residues 325 to 356) was determined at 1.7 angstrom resolution and, refined to a crystallographic R factor of 19.2 percent. The monomer, which, consists of a beta strand and an alpha helix, associates with a second, monomer across an antiparallel beta sheet and an antiparallel helix-helix, interface to form a dimer. Two of these dimers associate across a second, and distinct parallel helix-helix interface to form the tetramer.

The p53 protein is a tetrameric transcription factor that plays a central role in the prevention of neoplastic transformation. Oligomerization appears to be essential for the tumor suppressing activity of p53 because oligomerization-deficient p53 mutants cannot suppress the growth of carcinoma cell lines. The crystal structure of the tetramerization domain of p53 (residues 325 to 356) was determined at 1.7 angstrom resolution and refined to a crystallographic R factor of 19.2 percent. The monomer, which consists of a beta strand and an alpha helix, associates with a second monomer across an antiparallel beta sheet and an antiparallel helix-helix interface to form a dimer. Two of these dimers associate across a second and distinct parallel helix-helix interface to form the tetramer.

==Disease==

Line 11:

Line 10:

==About this Structure==

1C26 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=1C26 OCA].

1C26 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=1C26 OCA].

==Reference==

Line 18:

Line 17:

[[Category: Single protein]]

[[Category: Gorina, S.]]

[[Category: Jeffrey, P.D.]]

[[Category: Jeffrey, P D.]]

[[Category: Pavletich, N.P.]]

[[Category: Pavletich, N P.]]

[[Category: tetramer]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 16:16:~~54 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:37 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1c26.gif|left|200px]]<br />
+[[Image:1c26.gif|left|200px]]<br /><applet load="1c26" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1c26" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1c26, resolution 1.7&Aring;" />
 '''CRYSTAL STRUCTURE OF P53 TETRAMERIZATION DOMAIN'''<br />
 ==Overview==
-The p53 protein is a tetrameric transcription factor that plays a central, role in the prevention of neoplastic transformation. Oligomerization, appears to be essential for the tumor suppressing activity of p53 because, oligomerization-deficient p53 mutants cannot suppress the growth of, carcinoma cell lines. The crystal structure of the tetramerization domain, of p53 (residues 325 to 356) was determined at 1.7 angstrom resolution and, refined to a crystallographic R factor of 19.2 percent. The monomer, which, consists of a beta strand and an alpha helix, associates with a second, monomer across an antiparallel beta sheet and an antiparallel helix-helix, interface to form a dimer. Two of these dimers associate across a second, and distinct parallel helix-helix interface to form the tetramer.
+The p53 protein is a tetrameric transcription factor that plays a central role in the prevention of neoplastic transformation. Oligomerization appears to be essential for the tumor suppressing activity of p53 because oligomerization-deficient p53 mutants cannot suppress the growth of carcinoma cell lines. The crystal structure of the tetramerization domain of p53 (residues 325 to 356) was determined at 1.7 angstrom resolution and refined to a crystallographic R factor of 19.2 percent. The monomer, which consists of a beta strand and an alpha helix, associates with a second monomer across an antiparallel beta sheet and an antiparallel helix-helix interface to form a dimer. Two of these dimers associate across a second and distinct parallel helix-helix interface to form the tetramer.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-C26 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=1C26 OCA].
+C26 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=1C26 OCA].
 ==Reference==
@@ Line 18: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Gorina, S.]]
-[[Category: Jeffrey, P.D.]]
+[[Category: Jeffrey, P D.]]
-[[Category: Pavletich, N.P.]]
+[[Category: Pavletich, N P.]]
 [[Category: tetramer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:16:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:37 2008''