1b72: Difference between revisions
New page: left|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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[[Image:1b72.gif|left|200px]]<br /> | [[Image:1b72.gif|left|200px]]<br /><applet load="1b72" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1b72, resolution 2.35Å" /> | caption="1b72, resolution 2.35Å" /> | ||
'''PBX1, HOMEOBOX PROTEIN HOX-B1/DNA TERNARY COMPLEX'''<br /> | '''PBX1, HOMEOBOX PROTEIN HOX-B1/DNA TERNARY COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
Hox homeodomain proteins are developmental regulators that determine body | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1B72 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1B72 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B72 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Batchelor, A | [[Category: Batchelor, A H.]] | ||
[[Category: Chang, C | [[Category: Chang, C P.]] | ||
[[Category: Cleary, M | [[Category: Cleary, M L.]] | ||
[[Category: Piper, D | [[Category: Piper, D E.]] | ||
[[Category: Wolberger, C.]] | [[Category: Wolberger, C.]] | ||
[[Category: complex]] | [[Category: complex]] | ||
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[[Category: homeodomain]] | [[Category: homeodomain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:12 2008'' | ||
Revision as of 12:52, 21 February 2008
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PBX1, HOMEOBOX PROTEIN HOX-B1/DNA TERNARY COMPLEX
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Colorectal cancer OMIM:[604584], Hepatocellular cancer OMIM:[604584], Leukemia, acute pre-B-cell OMIM:[176310]
About this StructureAbout this Structure
1B72 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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