1du6
From Proteopedia
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| - | [[Image:1du6.jpg|left|200px]] | + | [[Image:1du6.jpg|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF THE TRUNCATED PBX HOMEODOMAIN''' | + | {{Structure |
| + | |PDB= 1du6 |SIZE=350|CAPTION= <scene name='initialview01'>1du6</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= PBX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF THE TRUNCATED PBX HOMEODOMAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DU6 is a [ | + | 1DU6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DU6 OCA]. |
==Reference== | ==Reference== | ||
| - | Conformational changes in the PBX homeodomain and C-terminal extension upon binding DNA and HOX-derived YPWM peptides., Sprules T, Green N, Featherstone M, Gehring K, Biochemistry. 2000 Aug 15;39(32):9943-50. PMID:[http:// | + | Conformational changes in the PBX homeodomain and C-terminal extension upon binding DNA and HOX-derived YPWM peptides., Sprules T, Green N, Featherstone M, Gehring K, Biochemistry. 2000 Aug 15;39(32):9943-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10933814 10933814] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: homeodomain]] | [[Category: homeodomain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:23 2008'' |
Revision as of 08:44, 20 March 2008
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| Gene: | PBX1 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE TRUNCATED PBX HOMEODOMAIN
Overview
PBX is a member of the three amino acid loop extension (TALE) class of homeodomains. PBX binds DNA cooperatively with HOX homeodomain proteins that contain a conserved YPWM motif. The amino acids immediately C-terminal to the PBX homeodomain increase the affinity of the homeodomain for its DNA site and HOX proteins. We have determined the structure of the free PBX homeodomain using NMR spectroscopy. Both the PBX homeodomain and the extended PBX homeodomain make identical contacts with a 5'-TGAT-3' DNA site and a YPWM peptide. A fourth alpha-helix, which forms upon binding to DNA, stabilizes the extended PBX structure. Variations in DNA sequence selectivity of heterodimeric PBX-HOX complexes depend on the HOX partner; however, a comparison of five different HOX-derived YPWM peptides showed that each bound to PBX in the same way, differing only in the strength of the association.
About this Structure
1DU6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Conformational changes in the PBX homeodomain and C-terminal extension upon binding DNA and HOX-derived YPWM peptides., Sprules T, Green N, Featherstone M, Gehring K, Biochemistry. 2000 Aug 15;39(32):9943-50. PMID:10933814
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