1an2: Difference between revisions

Revision as of 17:11, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1an2.png

Template:STRUCTURE 1an2

RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAINRECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN

Template:ABSTRACT PUBMED 8479534

About this StructureAbout this Structure

1AN2 is a Single protein structure. Full crystallographic information is available from OCA.

ReferenceReference

Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain., Ferre-D'Amare AR, Prendergast GC, Ziff EB, Burley SK, Nature. 1993 May 6;363(6424):38-45. PMID:8479534

Page seeded by OCA on Mon Jun 30 17:11:54 2008

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OCA

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-'''RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN'''
+===RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN===
-==Overview==
+<!--
-The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 A resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.
+The line below this paragraph, {{ABSTRACT_PUBMED_8479534}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8479534 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8479534}}
 ==About this Structure==
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 [[Category: Double helix]]
 [[Category: Protein-dna complex]]
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