2h1k: Difference between revisions

Revision as of 14:20, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2h1k.png

2h1k, resolution 2.42Å ()

Gene:

IPF1, PDX1 (Mesocricetus auratus)

Structural annotation:
Resources:	InterPro : Ipr012287, Ipr009057, Ipr001356, Ipr001827, Ipr000047 Pfam : PF00046 UniProt : P70118

Functional annotation:
Cellular component:	nucleus
Biological process:	regulation of transcription regulation of transcription, DNA-dependent transcription
Molecular function:	DNA binding transcription factor activity sequence-specific DNA binding

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

Crystal structure of the Pdx1 homeodomain in complex with DNACrystal structure of the Pdx1 homeodomain in complex with DNA

Template:ABSTRACT PUBMED 17315980

About this StructureAbout this Structure

2H1K is a Single protein structure of sequence from Mesocricetus auratus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for induced fit mechanisms in DNA recognition by the Pdx1 homeodomain., Longo A, Guanga GP, Rose RB, Biochemistry. 2007 Mar 20;46(11):2948-57. Epub 2007 Feb 23. PMID:17315980

Page seeded by OCA on Sun Jul 27 14:20:32 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of the Pdx1 homeodomain in complex with DNA'''
+===Crystal structure of the Pdx1 homeodomain in complex with DNA===
-==Overview==
+<!--
-Pancreatic and duodenal homeobox 1 (Pdx1) is a homeodomain transcription factor belonging to the ParaHox family. Pdx1 plays an essential role in pancreatic endocrine and exocrine cell development and maintenance of adult islet beta-cell function. Mutations in the human pdx1 gene are linked to an early onset form of non-insulin-dependent diabetes mellitus, MODY-4. We demonstrate that the homeodomain reproduces the binding specificity of the full-length protein. We report the 2.4 A resolution crystal structure of the homeodomain bound to a target DNA. The two Pdx1/DNA complexes in the asymmetric unit display conformational differences: in the DNA curvature, the orientation of the homeodomain in the major groove, and the order of the N-terminal arm. Comparing the two complexes indicates invariant protein-DNA contacts, and variant contacts that are unique to each binding orientation. An induced fit model is proposed that depends on the DNA conformation and provides a mechanism for nonlocal contributions to binding specificity.
+The line below this paragraph, {{ABSTRACT_PUBMED_17315980}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17315980 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17315980}}
 ==About this Structure==
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 [[Category: Rose, R B.]]
 [[Category: Protein-dna complex]]
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