2dgc
From Proteopedia
(New page: 200px<br /><applet load="2dgc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dgc, resolution 2.200Å" /> '''GCN4 BASIC DOMAIN, ...) |
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| - | [[Image:2dgc.gif|left|200px]]<br /><applet load="2dgc" size=" | + | [[Image:2dgc.gif|left|200px]]<br /><applet load="2dgc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2dgc, resolution 2.200Å" /> | caption="2dgc, resolution 2.200Å" /> | ||
'''GCN4 BASIC DOMAIN, LEUCINE ZIPPER COMPLEXED WITH ATF/CREB SITE DNA'''<br /> | '''GCN4 BASIC DOMAIN, LEUCINE ZIPPER COMPLEXED WITH ATF/CREB SITE DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray structure of the GCN4-bZIP protein bound to DNA containing the | + | 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== | ==About this Structure== | ||
| - | 2DGC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 2DGC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DGC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Keller, W.]] | [[Category: Keller, W.]] | ||
[[Category: Koenig, P.]] | [[Category: Koenig, P.]] | ||
| - | [[Category: Richmond, T | + | [[Category: Richmond, T J.]] |
[[Category: basic domain]] | [[Category: basic domain]] | ||
[[Category: dna binding]] | [[Category: dna binding]] | ||
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[[Category: leucine zipper]] | [[Category: leucine zipper]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:58:31 2008'' |
Revision as of 14:58, 21 February 2008
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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
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