1hdd: Difference between revisions

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New page: left|200px<br /><applet load="1hdd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hdd, resolution 2.800Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1hdd.jpg|left|200px]]<br /><applet load="1hdd" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hdd.jpg|left|200px]]<br /><applet load="1hdd" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hdd, resolution 2.800&Aring;" />
caption="1hdd, resolution 2.800&Aring;" />
'''CRYSTAL STRUCTURE OF AN ENGRAILED HOMEODOMAIN-DNA COMPLEX AT 2.8 ANGSTROMS RESOLUTION: A FRAMEWORK FOR UNDERSTANDING HOMEODOMAIN-DNA INTERACTIONS'''<br />
'''CRYSTAL STRUCTURE OF AN ENGRAILED HOMEODOMAIN-DNA COMPLEX AT 2.8 ANGSTROMS RESOLUTION: A FRAMEWORK FOR UNDERSTANDING HOMEODOMAIN-DNA INTERACTIONS'''<br />


==Overview==
==Overview==
The crystal structure of a complex containing the engrailed homeodomain, and a duplex DNA site has been determined at 2.8 A resolution and refined, to a crystallographic R factor of 24.4%. In this complex, two separate, regions of the 61 amino acid polypeptide contact a TAAT subsite. An, N-terminal arm fits into the minor groove, and the side chains of Arg-3, and Arg-5 make contacts near the 5' end of this "core consensus" binding, site. An alpha helix fits into the major groove, and the side chains of, IIe-47 and Asn-51 contact base pairs near the 3' end of the TAAT site., This "recognition helix" is part of a structurally conserved, helix-turn-helix unit, but these helices are longer than the corresponding, helices in the lambda repressor, and the relationship between the, helix-turn-helix unit and the DNA is significantly different.
The crystal structure of a complex containing the engrailed homeodomain and a duplex DNA site has been determined at 2.8 A resolution and refined to a crystallographic R factor of 24.4%. In this complex, two separate regions of the 61 amino acid polypeptide contact a TAAT subsite. An N-terminal arm fits into the minor groove, and the side chains of Arg-3 and Arg-5 make contacts near the 5' end of this "core consensus" binding site. An alpha helix fits into the major groove, and the side chains of IIe-47 and Asn-51 contact base pairs near the 3' end of the TAAT site. This "recognition helix" is part of a structurally conserved helix-turn-helix unit, but these helices are longer than the corresponding helices in the lambda repressor, and the relationship between the helix-turn-helix unit and the DNA is significantly different.


==About this Structure==
==About this Structure==
1HDD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HDD OCA].  
1HDD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HDD OCA].  


==Reference==
==Reference==
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[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Kissinger, C.R.]]
[[Category: Kissinger, C R.]]
[[Category: Liu, B.]]
[[Category: Liu, B.]]
[[Category: Martin-Blanco, E.]]
[[Category: Martin-Blanco, E.]]
[[Category: Pabo, T.B.Kornberg C.O.]]
[[Category: Pabo, T B.Kornberg C O.]]
[[Category: double helix]]
[[Category: double helix]]
[[Category: protein-dna complex]]
[[Category: protein-dna complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:32:03 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:13 2008''

Revision as of 14:00, 21 February 2008

File:1hdd.jpg


1hdd, resolution 2.800Å

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CRYSTAL STRUCTURE OF AN ENGRAILED HOMEODOMAIN-DNA COMPLEX AT 2.8 ANGSTROMS RESOLUTION: A FRAMEWORK FOR UNDERSTANDING HOMEODOMAIN-DNA INTERACTIONS

OverviewOverview

The crystal structure of a complex containing the engrailed homeodomain and a duplex DNA site has been determined at 2.8 A resolution and refined to a crystallographic R factor of 24.4%. In this complex, two separate regions of the 61 amino acid polypeptide contact a TAAT subsite. An N-terminal arm fits into the minor groove, and the side chains of Arg-3 and Arg-5 make contacts near the 5' end of this "core consensus" binding site. An alpha helix fits into the major groove, and the side chains of IIe-47 and Asn-51 contact base pairs near the 3' end of the TAAT site. This "recognition helix" is part of a structurally conserved helix-turn-helix unit, but these helices are longer than the corresponding helices in the lambda repressor, and the relationship between the helix-turn-helix unit and the DNA is significantly different.

About this StructureAbout this Structure

1HDD is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of an engrailed homeodomain-DNA complex at 2.8 A resolution: a framework for understanding homeodomain-DNA interactions., Kissinger CR, Liu BS, Martin-Blanco E, Kornberg TB, Pabo CO, Cell. 1990 Nov 2;63(3):579-90. PMID:1977522

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