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.


2drp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2drp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2drp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2drp| PDB=2drp | SCENE= }}
{{STRUCTURE_2drp| PDB=2drp | SCENE= }}
-
'''THE CRYSTAL STRUCTURE OF A TWO ZINC-FINGER PEPTIDE REVEALS AN EXTENSION TO THE RULES FOR ZINC-FINGER/DNA RECOGNITION'''
+
===THE CRYSTAL STRUCTURE OF A TWO ZINC-FINGER PEPTIDE REVEALS AN EXTENSION TO THE RULES FOR ZINC-FINGER/DNA RECOGNITION===
-
==Overview==
+
<!--
-
The Cys2-His2 zinc-finger is the most widely occurring DNA-binding motif. The first structure of a zinc-finger/DNA complex revealed a fairly simple mechanism for DNA recognition suggesting that the zinc-finger might represent a candidate template for designing proteins to recognize DNA. Residues at three key positions in an alpha-helical 'reading head' play a dominant role in base-recognition and have been targets for mutagenesis experiments aimed at deriving a recognition code. Here we report the structure of a two zinc-finger DNA-binding domain from the protein Tramtrack complexed with DNA. The amino-terminal zinc-finger and its interaction with DNA illustrate several novel features. These include the use of a serine residue, which is semi-conserved and located outside the three key positions, to make a base contact. Its role in base-recognition correlates with a large, local, protein-induced deformation of the DNA helix at a flexible A-T-A sequence and may give insight into previous mutagenesis experiments. It is apparent from this structure that zinc-finger/DNA recognition is more complex than was originally perceived.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8247159}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8247159 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8247159}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Double helix]]
[[Category: Double helix]]
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:01:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:15:02 2008''

Revision as of 12:15, 27 July 2008

Image:2drp.png

Template:STRUCTURE 2drp

THE CRYSTAL STRUCTURE OF A TWO ZINC-FINGER PEPTIDE REVEALS AN EXTENSION TO THE RULES FOR ZINC-FINGER/DNA RECOGNITION

Template:ABSTRACT PUBMED 8247159

About this Structure

2DRP is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition., Fairall L, Schwabe JW, Chapman L, Finch JT, Rhodes D, Nature. 1993 Dec 2;366(6454):483-7. PMID:8247159

Page seeded by OCA on Sun Jul 27 15:15:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2drp"
Personal tools