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1g2z

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{{STRUCTURE_1g2z| PDB=1g2z | SCENE= }}
{{STRUCTURE_1g2z| PDB=1g2z | SCENE= }}
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'''DIMERIZATION DOMAIN OF HNF-1ALPHA WITH A LEU 13 SELENOMETHIONINE SUBSTITUTION'''
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===DIMERIZATION DOMAIN OF HNF-1ALPHA WITH A LEU 13 SELENOMETHIONINE SUBSTITUTION===
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11106484 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11106484}}
==About this Structure==
==About this Structure==
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[[Category: Selenomethionine]]
[[Category: Selenomethionine]]
[[Category: Transcription factor]]
[[Category: Transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:20:09 2008''

Revision as of 01:20, 1 July 2008

Image:1g2z.png

Template:STRUCTURE 1g2z

DIMERIZATION DOMAIN OF HNF-1ALPHA WITH A LEU 13 SELENOMETHIONINE SUBSTITUTION

Template:ABSTRACT PUBMED 11106484

About this Structure

1G2Z 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 04:20:09 2008

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