1f93

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(New page: 200px<br /><applet load="1f93" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f93, resolution 2.60&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1f93.gif|left|200px]]<br /><applet load="1f93" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1f93.gif|left|200px]]<br /><applet load="1f93" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1f93, resolution 2.60&Aring;" />
caption="1f93, resolution 2.60&Aring;" />
'''CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH'''<br />
'''CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH'''<br />
==Overview==
==Overview==
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Maturity-onset diabetes of the young type 3 (MODY3) results from mutations, in the transcriptional activator hepatocyte nuclear factor-1alpha, (HNF-1alpha). Several MODY3 mutations target the HNF-1alpha dimerization, domain (HNF-p1), which binds the coactivator, dimerization cofactor of, HNF-1 (DCoH). To define the mechanism of coactivator recognition and the, basis for the MODY3 phenotype, we determined the cocrystal structure of, the DCoH-HNF-p1 complex and characterized biochemically the effects of, MODY3 mutations in HNF-p1. The DCoH-HNF-p1 complex comprises a dimer of, dimers in which HNF-p1 forms a unique four-helix bundle. Through, rearrangements of interfacial side chains, a single, bifunctional, interface in the DCoH dimer mediates both HNF-1alpha binding and formation, of a competing, transcriptionally inactive DCoH homotetramer. Consistent, with the structure, MODY3 mutations in HNF-p1 reduce activator function by, two distinct mechanisms.
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Maturity-onset diabetes of the young type 3 (MODY3) results from mutations in the transcriptional activator hepatocyte nuclear factor-1alpha (HNF-1alpha). Several MODY3 mutations target the HNF-1alpha dimerization domain (HNF-p1), which binds the coactivator, dimerization cofactor of HNF-1 (DCoH). To define the mechanism of coactivator recognition and the basis for the MODY3 phenotype, we determined the cocrystal structure of the DCoH-HNF-p1 complex and characterized biochemically the effects of MODY3 mutations in HNF-p1. The DCoH-HNF-p1 complex comprises a dimer of dimers in which HNF-p1 forms a unique four-helix bundle. Through rearrangements of interfacial side chains, a single, bifunctional interface in the DCoH dimer mediates both HNF-1alpha binding and formation of a competing, transcriptionally inactive DCoH homotetramer. Consistent with the structure, MODY3 mutations in HNF-p1 reduce activator function by two distinct mechanisms.
==About this Structure==
==About this Structure==
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1F93 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F93 OCA].
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1F93 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F93 OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Alber, T.]]
[[Category: Alber, T.]]
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[[Category: Bayle, J.H.]]
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[[Category: Bayle, J H.]]
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[[Category: Crabtree, G.R.]]
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[[Category: Crabtree, G R.]]
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[[Category: Cronk, J.D.]]
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[[Category: Cronk, J D.]]
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[[Category: Endrizzi, J.A.]]
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[[Category: Endrizzi, J A.]]
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[[Category: Rose, R.B.]]
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[[Category: Rose, R B.]]
[[Category: dimerization domain]]
[[Category: dimerization domain]]
[[Category: four-helix bundle]]
[[Category: four-helix bundle]]
[[Category: transcriptional activator/coactivator complex]]
[[Category: transcriptional activator/coactivator complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:43:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:09 2008''

Revision as of 10:36, 21 February 2008

Image:1f93.gif

1f93, resolution 2.60Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE DIMERIZATION DOMAIN OF HNF-1 ALPHA AND THE COACTIVATOR DCOH

Overview

Maturity-onset diabetes of the young type 3 (MODY3) results from mutations in the transcriptional activator hepatocyte nuclear factor-1alpha (HNF-1alpha). Several MODY3 mutations target the HNF-1alpha dimerization domain (HNF-p1), which binds the coactivator, dimerization cofactor of HNF-1 (DCoH). To define the mechanism of coactivator recognition and the basis for the MODY3 phenotype, we determined the cocrystal structure of the DCoH-HNF-p1 complex and characterized biochemically the effects of MODY3 mutations in HNF-p1. The DCoH-HNF-p1 complex comprises a dimer of dimers in which HNF-p1 forms a unique four-helix bundle. Through rearrangements of interfacial side chains, a single, bifunctional interface in the DCoH dimer mediates both HNF-1alpha binding and formation of a competing, transcriptionally inactive DCoH homotetramer. Consistent with the structure, MODY3 mutations in HNF-p1 reduce activator function by two distinct mechanisms.

About this Structure

1F93 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structural basis of dimerization, coactivator recognition and MODY3 mutations in HNF-1alpha., Rose RB, Bayle JH, Endrizzi JA, Cronk JD, Crabtree GR, Alber T, Nat Struct Biol. 2000 Sep;7(9):744-8. PMID:10966642

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