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| - | [[Image:1g2y.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1g2y.png|left|200px]] |
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| | {{STRUCTURE_1g2y| PDB=1g2y | SCENE= }} | | {{STRUCTURE_1g2y| PDB=1g2y | SCENE= }} |
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| - | '''HNF-1ALPHA DIMERIZATION DOMAIN, WITH SELENOMETHIONINE SUBSTITUED AT LEU 12'''
| + | ===HNF-1ALPHA DIMERIZATION DOMAIN, WITH SELENOMETHIONINE SUBSTITUED AT LEU 12=== |
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| - | ==Overview==
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| - | The N-terminal dimerization domain of the transcriptional activator hepatocyte nuclear factor-1alpha (HNF-1alpha) is essential for DNA binding and association of the transcriptional coactivator, DCoH (dimerization cofactor of HNF-1). To investigate the basis for dimerization of HNF-1 proteins, we determined the 1.2 A resolution X-ray crystal structure of the dimerization domain of HNF-1alpha (HNF-p1). Phasing was facilitated by devising a simple synthesis for Fmoc-selenomethionine and substituting leucine residues with selenomethionine. The HNF-1 dimerization domain forms a unique, four-helix bundle that is preserved with localized conformational shifts in the DCoH complex. In three different crystal forms, HNF-p1 displays subtle shifts in the conformation of the interhelix loop and the crossing angle between the amino- and carboxyl-terminal helices. In all three crystal forms, the HNF-p1 dimers pair through an exposed hydrophobic surface that also forms the binding site for DCoH. Conserved core residues in the dimerization domain of the homologous transcriptional regulator HNF-1beta rationalize the functional heterodimerization of the HNF-1alpha and HNF-1beta proteins. Mutations in HNF-1alpha are associated with maturity-onset diabetes of the young type 3 (MODY3), and the structure of HNF-p1 provides insights into the effects of three MODY3 mutations. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11106484}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11106484 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11106484}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Selenomethionine]] | | [[Category: Selenomethionine]] |
| | [[Category: Transcription factor]] | | [[Category: Transcription factor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:04:25 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:20:13 2008'' |
Revision as of 01:20, 1 July 2008
Template:STRUCTURE 1g2y
HNF-1ALPHA DIMERIZATION DOMAIN, WITH SELENOMETHIONINE SUBSTITUED AT LEU 12
Template:ABSTRACT PUBMED 11106484
About this Structure
1G2Y is a Single protein structure. Full crystallographic information is available from OCA.
Reference
High-resolution structure of the HNF-1alpha dimerization domain., Rose RB, Endrizzi JA, Cronk JD, Holton J, Alber T, Biochemistry. 2000 Dec 12;39(49):15062-70. PMID:11106484
Page seeded by OCA on Tue Jul 1 04:20:13 2008
