2dgc
From Proteopedia
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[[Image:2dgc.gif|left|200px]] | [[Image:2dgc.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_2dgc| PDB=2dgc | SCENE= }} | |
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'''GCN4 BASIC DOMAIN, LEUCINE ZIPPER COMPLEXED WITH ATF/CREB SITE DNA''' | '''GCN4 BASIC DOMAIN, LEUCINE ZIPPER COMPLEXED WITH ATF/CREB SITE DNA''' | ||
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[[Category: Koenig, P.]] | [[Category: Koenig, P.]] | ||
[[Category: Richmond, T J.]] | [[Category: Richmond, T J.]] | ||
| - | [[Category: | + | [[Category: Basic domain]] |
| - | [[Category: | + | [[Category: Dna binding]] |
| - | [[Category: | + | [[Category: Eukaryotic regulatory protein]] |
| - | [[Category: | + | [[Category: Leucine zipper]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:22:04 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:22, 3 May 2008
GCN4 BASIC DOMAIN, LEUCINE ZIPPER COMPLEXED WITH ATF/CREB SITE DNA
Overview
The X-ray structure of the GCN4-bZIP protein bound to DNA containing the ATF/CREB recognition sequence has been refined at 2.2 A. The water-mediated interactions between the basic domain and DNA are revealed, and combined with a more accurate description of the direct contacts, further clarify how binding specificity is achieved. Water molecules extend the interactions of both invariant basic domain residues, asparagine 235 and arginine 243, beyond their direct base contacts. The slight bending of the basic domain alpha-helix around the DNA facilitates the linking of arginine 241, 243 and 245 to main-chain carbonyl oxygen atoms via water molecules, apparently stabilizing interactions with the DNA.
About this Structure
2DGC is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of a bZIP/DNA complex at 2.2 A: determinants of DNA specific recognition., Keller W, Konig P, Richmond TJ, J Mol Biol. 1995 Dec 8;254(4):657-67. PMID:7500340 Page seeded by OCA on Sun May 4 00:22:04 2008
