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.


1sah

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sah.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1sah.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sah| PDB=1sah | SCENE= }}
{{STRUCTURE_1sah| PDB=1sah | SCENE= }}
-
'''HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR (SAD STRUCTURES)'''
+
===HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR (SAD STRUCTURES)===
-
==Overview==
+
<!--
-
The NMR solution structure of the oligomerization domain of the tumour suppressor p53 (residues 319-360) has been refined. The structure comprises a dimer of dimers, oriented in an approximately orthogonal manner. The present structure determination is based on 4,472 experimental NMR restraints which represents a three and half fold increase over our previous work in the number of NOE restraints at the tetramerization interface. A comparison with the recently solved 1.7 A resolution X-ray structure shows that the structures are very similar and that the average angular root-mean-square difference in the interhelical angles is about 1 degree. The results of recent extensive mutagenesis data and the possible effects of mutations which have been identified in human cancers are discussed in the light of the present structure.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7796267}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7796267 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7796267}}
==About this Structure==
==About this Structure==
-
1SAH 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=1SAH OCA].
+
1SAH 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=1SAH OCA].
==Reference==
==Reference==
Line 26: Line 30:
[[Category: Omichinski, J G.]]
[[Category: Omichinski, J G.]]
[[Category: Anti-oncogene]]
[[Category: Anti-oncogene]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:29:07 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:45:22 2008''

Revision as of 18:45, 27 July 2008

Image:1sah.png

Template:STRUCTURE 1sah

HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR (SAD STRUCTURES)

Template:ABSTRACT PUBMED 7796267

About this Structure

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

Reference

Refined solution structure of the oligomerization domain of the tumour suppressor p53., Clore GM, Ernst J, Clubb R, Omichinski JG, Kennedy WM, Sakaguchi K, Appella E, Gronenborn AM, Nat Struct Biol. 1995 Apr;2(4):321-33. PMID:7796267

Page seeded by OCA on Sun Jul 27 21:45:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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