1odh: Difference between revisions
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[[Image:1odh.gif|left|200px]] | [[Image:1odh.gif|left|200px]] | ||
'''STRUCTURE OF THE GCM DOMAIN BOUND TO DNA''' | {{Structure | ||
|PDB= 1odh |SIZE=350|CAPTION= <scene name='initialview01'>1odh</scene>, resolution 2.85Å | |||
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF THE GCM DOMAIN BOUND TO DNA''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ODH is a [ | 1ODH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODH OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the GCM domain-DNA complex: a DNA-binding domain with a novel fold and mode of target site recognition., Cohen SX, Moulin M, Hashemolhosseini S, Kilian K, Wegner M, Muller CW, EMBO J. 2003 Apr 15;22(8):1835-45. PMID:[http:// | Structure of the GCM domain-DNA complex: a DNA-binding domain with a novel fold and mode of target site recognition., Cohen SX, Moulin M, Hashemolhosseini S, Kilian K, Wegner M, Muller CW, EMBO J. 2003 Apr 15;22(8):1835-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12682016 12682016] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:09:21 2008'' | ||
Revision as of 14:09, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE GCM DOMAIN BOUND TO DNA
OverviewOverview
Glia cell missing (GCM) transcription factors form a small family of transcriptional regulators in metazoans. The prototypical Drosophila GCM protein directs the differentiation of neuron precursor cells into glia cells, whereas mammalian GCM proteins are involved in placenta and parathyroid development. GCM proteins share a highly conserved 150 amino acid residue region responsible for DNA binding, known as the GCM domain. Here we present the crystal structure of the GCM domain from murine GCMa bound to its octameric DNA target site at 2.85 A resolution. The GCM domain exhibits a novel fold consisting of two domains tethered together by one of two structural Zn ions. We observe the novel use of a beta-sheet in DNA recognition, whereby a five- stranded beta-sheet protrudes into the major groove perpendicular to the DNA axis. The structure combined with mutational analysis of the target site and of DNA-contacting residues provides insight into DNA recognition by this new type of Zn-containing DNA-binding domain.
About this StructureAbout this Structure
1ODH is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the GCM domain-DNA complex: a DNA-binding domain with a novel fold and mode of target site recognition., Cohen SX, Moulin M, Hashemolhosseini S, Kilian K, Wegner M, Muller CW, EMBO J. 2003 Apr 15;22(8):1835-45. PMID:12682016
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