Source:http://linkedlifedata.com/resource/umls/id/C0949662
MSH: DNA-binding motifs, first described in one of the HMGA PROTEINS: HMG-I(Y) PROTEIN. They consist of positively charged sequences of nine amino acids centered on the invariant tripeptide glycine-arginine-proline. They act to fasten the protein to an AT RICH SEQUENCE in the DNA.,NCI: Highly conserved peptide motifs of the HMG-I(Y) proteins that preferentially bind to the AT-rich minor groove of DNA. The AT hook motif tethers and unwinds the minor groove of the DNA with very little specificity for the DNA sequence. The AT hook motif has a narrow DNA recognition surface that is devoid of hydrophobic amino acids and that does not significantly distort the B-form DNA structure.,NCI: Highly conserved peptide motifs of the HMG-I(Y) proteins that preferentially bind, in vivo and in vitro, to the narrow minor groove of stretches of AT-rich DNA. The AT Hook Motif tethers and unbends the minor groove of the DNA with very little specificity for the DNA sequence. The AT hook motif has a narrow DNA recognize surface whi