Brachyury: Difference between revisions
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Two well-known orthologues of the <i>Homo sapiens</i> T protein are present in mice (Brachyury) and <i>Xenopus laevis</i> (Xbra). The homologue of T in mice, Brachyury, was the first T-box crystal structure to be determined. | Two well-known orthologues of the <i>Homo sapiens</i> T protein are present in mice (Brachyury) and <i>Xenopus laevis</i> (Xbra). The homologue of T in mice, Brachyury, was the first T-box crystal structure to be determined. | ||
=Crystal structure= | =Crystal structure ([[1xbr]])= | ||
The T-box region of the Brachyury protein was crystallised with a 24 bp palindromic DNA duplex as determined by <i>in vitro</i> PCR-based binding selection. It crystallised as a dimer; in one monomer residues 39-221 were visible out of a total of 226 residues, and in the other residues 39-222 were visible. Both monomers were bound to the DNA (unlike in the structure of [[TBX5]]) and interacted through a poorly conserved region of 250 Å<sup>2</sup>. The N-terminus of 38 residues and C-terminus of 4 residues were disordered in the crystal structure. Nevertheless, the crystallographic structure agrees with DNA footprinting experiments in terms of which bases are protected by the protein. | The T-box region of the Brachyury protein was crystallised with a 24 bp palindromic DNA duplex as determined by <i>in vitro</i> PCR-based binding selection. It crystallised as a dimer; in one monomer residues 39-221 were visible out of a total of 226 residues, and in the other residues 39-222 were visible. Both monomers were bound to the DNA (unlike in the structure of [[TBX5]]) and interacted through a poorly conserved region of 250 Å<sup>2</sup>. The N-terminus of 38 residues and C-terminus of 4 residues were disordered in the crystal structure. Nevertheless, the crystallographic structure agrees with DNA footprinting experiments in terms of which bases are protected by the protein. | ||