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.


1yrn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1yrn.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1yrn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1yrn| PDB=1yrn | SCENE= }}
{{STRUCTURE_1yrn| PDB=1yrn | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE MATA1/MATALPHA2 HOMEODOMAIN HETERODIMER BOUND TO DNA'''
+
===CRYSTAL STRUCTURE OF THE MATA1/MATALPHA2 HOMEODOMAIN HETERODIMER BOUND TO DNA===
-
==Overview==
+
<!--
-
The Saccharomyces cerevisiae MATa1 and MAT alpha 2 homeodomain proteins, which play a role in determining yeast cell type, form a heterodimer that binds DNA and represses transcription in a cell type-specific manner. Whereas the alpha 2 and a1 proteins on their own have only modest affinity for DNA, the a1/alpha 2 heterodimer binds DNA with high specificity and affinity. The three-dimensional crystal structure of the a1/alpha 2 homeodomain heterodimer bound to DNA was determined at a resolution of 2.5 A. The a1 and alpha 2 homeodomains bind in a head-to-tail orientation, with heterodimer contacts mediated by a 16-residue tail located carboxyl-terminal to the alpha 2 homeodomain. This tail becomes ordered in the presence of a1, part of it forming a short amphipathic helix that packs against the a1 homeodomain between helices 1 and 2. A pronounced 60 degree bend is induced in the DNA, which makes possible protein-protein and protein-DNA contacts that could not take place in a straight DNA fragment. Complex formation mediated by flexible protein-recognition peptides attached to stably folded DNA binding domains may prove to be a general feature of the architecture of other classes of eukaryotic transcriptional regulators.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7569974}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7569974 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7569974}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Dna]]
[[Category: Dna]]
[[Category: Dna-binding protein]]
[[Category: Dna-binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:41:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:53:23 2008''

Revision as of 08:53, 28 July 2008

Image:1yrn.png

Template:STRUCTURE 1yrn

CRYSTAL STRUCTURE OF THE MATA1/MATALPHA2 HOMEODOMAIN HETERODIMER BOUND TO DNA

Template:ABSTRACT PUBMED 7569974

About this Structure

1YRN is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA., Li T, Stark MR, Johnson AD, Wolberger C, Science. 1995 Oct 13;270(5234):262-9. PMID:7569974

Page seeded by OCA on Mon Jul 28 11:53:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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