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.


1srk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1srk.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1srk.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1srk| PDB=1srk | SCENE= }}
{{STRUCTURE_1srk| PDB=1srk | SCENE= }}
-
'''Solution structure of the third zinc finger domain of FOG-1'''
+
===Solution structure of the third zinc finger domain of FOG-1===
-
==Overview==
+
<!--
-
Classic zinc finger domains (cZFs) consist of a beta-hairpin followed by an alpha-helix. They are among the most abundant of all protein domains and are often found in tandem arrays in DNA-binding proteins, with each finger contributing an alpha-helix to effect sequence-specific DNA recognition. Lone cZFs, not found in tandem arrays, have been postulated to function in protein interactions. We have studied the transcriptional co-regulator Friend of GATA (FOG), which contains nine zinc fingers. We have discovered that the third cZF of FOG contacts a coiled-coil domain in the centrosomal protein transforming acidic coiled-coil 3 (TACC3). Although FOG-ZF3 exhibited low solubility, we have used a combination of mutational mapping and protein engineering to generate a derivative that was suitable for in vitro and structural analysis. We report that the alpha-helix of FOG-ZF3 recognizes a C-terminal portion of the TACC3 coiled-coil. Remarkably, the alpha-helical surface utilized by FOG-ZF3 is the same surface responsible for the well established sequence-specific DNA-binding properties of many other cZFs. Our data demonstrate the versatility of cZFs and have implications for the analysis of many as yet uncharacterized cZF proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15234987}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15234987 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15234987}}
==About this Structure==
==About this Structure==
-
1SRK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRK OCA].
+
1SRK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRK OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Simpson, R J.Y.]]
[[Category: Simpson, R J.Y.]]
[[Category: Classical zinc finger]]
[[Category: Classical zinc finger]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:03:49 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:07:49 2008''

Revision as of 00:07, 29 July 2008

Template:STRUCTURE 1srk

Solution structure of the third zinc finger domain of FOG-1

Template:ABSTRACT PUBMED 15234987

About this Structure

1SRK is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.

Reference

A classic zinc finger from friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3., Simpson RJ, Yi Lee SH, Bartle N, Sum EY, Visvader JE, Matthews JM, Mackay JP, Crossley M, J Biol Chem. 2004 Sep 17;279(38):39789-97. Epub 2004 Jul 2. PMID:15234987

Page seeded by OCA on Tue Jul 29 03:07:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools