This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1hs5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hs5.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1hs5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hs5| PDB=1hs5 | SCENE= }}
{{STRUCTURE_1hs5| PDB=1hs5 | SCENE= }}
-
'''NMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER'''
+
===NMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER===
-
==Overview==
+
<!--
-
P53 is a homotetrameric tumor suppressor protein involved in transcriptional control of genes that regulate cell proliferation and death. In order to probe the role that oligomerization plays in this capacity, we have previously designed and characterized a series of p53 proteins with altered oligomeric states through hydrophilc substitution of residues Met340 or Leu344 in the normally tetrameric oligomerization domain. Although such mutations have little effect on the overall secondary structural content of the oligomerization domain, both solubility and the resistance to thermal denaturation are substantially reduced relative to that of the wild-type domain. Here, we report the design and characterization of a double-mutant p53 with alterations of residues at positions Met340 and Leu344. The double-mutations Met340Glu/Leu344Lys and Met340Gln/Leu344Arg resulted in distinct dimeric forms of the protein. Furthermore, we have verified by NMR structure determination that the double-mutant Met340Gln/Leu344Arg is essentially a "half-tetramer". Analysis of the in vivo activities of full-length p53 oligomeric mutants reveals that while cell-cycle arrest requires tetrameric p53, transcriptional transactivation activity of monomers and dimers retain roughly background and half of the wild-type activity, respectively.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11254385}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11254385 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11254385}}
==About this Structure==
==About this Structure==
-
1HS5 is a [[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=1HS5 OCA].
+
1HS5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HS5 OCA].
==Reference==
==Reference==
Line 31: Line 35:
[[Category: Anti-parallel beta-turn-helix]]
[[Category: Anti-parallel beta-turn-helix]]
[[Category: Dimer]]
[[Category: Dimer]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:10:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:36:39 2008''

Revision as of 05:36, 1 July 2008

Image:1hs5.png

Template:STRUCTURE 1hs5

NMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER

Template:ABSTRACT PUBMED 11254385

About this Structure

1HS5 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Structure and functionality of a designed p53 dimer., Davison TS, Nie X, Ma W, Lin Y, Kay C, Benchimol S, Arrowsmith CH, J Mol Biol. 2001 Mar 23;307(2):605-17. PMID:11254385

Page seeded by OCA on Tue Jul 1 08:36:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hs5"
Personal tools