1lfu Summary


NMR Solution Stucture of the Extended PBX Homeodomain Bound to DNA

The structure was published by Sprules, T., Green, N., Featherstone, M., and Gehring, K., in 2003 in a paper entitled "Lock and Key Binding of the HOX YPWM Peptide to the PBX Homeodomain" (abstract).

The structure was determined using NMR spectroscopy and deposited in 2002.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 3 biomacromolecules, namely 5'-D(*GP*CP*GP*CP*AP*TP*GP*AP*TP*TP*GP*CP*CP*C)-3', 5'-D(*GP*GP*GP*CP*AP*AP*TP*CP*AP*TP*GP*CP*GP*C)-3', and homeobox protein PBX1.

The molecule most likely forms heterotrimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
P homeobox protein PBX1 P41778 (233-313) (PBX1_MOUSE)search Mus musculussearch < 90% 82 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P41778 (233 - 313) homeobox protein PBX1 Mus musculus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
P Homeodomainsearch Homeodomain-likesearch Homeobox domainsearch

Chain ID Biological process (GO) Molecular function (GO)
P (P41778) regulation of transcription, DNA-templatedsearch DNA bindingsearch sequence-specific DNA bindingsearch

Chain InterPro annotation
P Homeobox domainsearch Homeodomain-likesearch Homeobox, conserved sitesearch