1b72
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(New page: 200px<br /> <applet load="1b72" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b72, resolution 2.35Å" /> '''PBX1, HOMEOBOX PROT...)
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Revision as of 14:00, 12 November 2007
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PBX1, HOMEOBOX PROTEIN HOX-B1/DNA TERNARY COMPLEX
Contents |
Overview
Hox homeodomain proteins are developmental regulators that determine body, plan in a variety of organisms. A majority of the vertebrate Hox proteins, bind DNA as heterodimers with the Pbx1 homeodomain protein. We report here, the 2.35 A structure of a ternary complex containing a human HoxB1-Pbx1, heterodimer bound to DNA. Heterodimer contacts are mediated by the, hexapeptide of HoxB1, which binds in a pocket in the Pbx1 protein formed, in part by a three-amino acid insertion in the Pbx1 homeodomain. The Pbx1, DNA-binding domain is larger than the canonical homeodomain, containing an, additional alpha helix that appears to contribute to binding of the HoxB1, hexapeptide and to stable binding of Pbx1 to DNA. The structure suggests a, model for modulation of Hox DNA binding activity by Pbx1 and related, proteins.
Disease
Known diseases associated with this structure: Colorectal cancer OMIM:[604584], Hepatocellular cancer OMIM:[604584], Leukemia, acute pre-B-cell OMIM:[176310]
About this Structure
1B72 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation., Piper DE, Batchelor AH, Chang CP, Cleary ML, Wolberger C, Cell. 1999 Feb 19;96(4):587-97. PMID:10052460
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