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.


1a1u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a1u.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1a1u.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1a1u| PDB=1a1u | SCENE= }}
{{STRUCTURE_1a1u| PDB=1a1u | SCENE= }}
-
'''SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE'''
+
===SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE===
-
==Overview==
+
<!--
-
The p53 tumor suppressor oligomerization domain, a dimer of two primary dimers, is an independently folding domain whose subunits consist of a beta-strand, a tight turn and an alpha-helix. To evaluate the effect of hydrophobic side-chains on three-dimensional structure, we substituted residues Phe341 and Leu344 in the alpha-helix with other hydrophobic amino acids. Substitutions that resulted in residue 341 having a smaller side-chain than residue 344 switched the stoichiometry of the domain from tetrameric to dimeric. The three-dimensional structure of one such dimer was determined by multidimensional NMR spectroscopy. When compared with the primary dimer of the wild-type p53 oligomerization domain, the mutant dimer showed a switch in alpha-helical packing from anti-parallel to parallel and rotation of the alpha-helices relative to the beta-strands. Hydrophobic side-chain size is therefore an important determinant of a protein fold.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9321402}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9321402 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9321402}}
==About this Structure==
==About this Structure==
-
1A1U 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=1A1U OCA].
+
1A1U 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=1A1U OCA].
==Reference==
==Reference==
Line 33: Line 37:
[[Category: Oligomerization domain]]
[[Category: Oligomerization domain]]
[[Category: P53]]
[[Category: P53]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:40:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:48:34 2008''

Revision as of 12:48, 30 June 2008

Template:STRUCTURE 1a1u

SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

Template:ABSTRACT PUBMED 9321402

About this Structure

1A1U is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain., McCoy M, Stavridi ES, Waterman JL, Wieczorek AM, Opella SJ, Halazonetis TD, EMBO J. 1997 Oct 15;16(20):6230-6. PMID:9321402

Page seeded by OCA on Mon Jun 30 15:48:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools