| Type: | Family | Name: | AT hook-like |
| Description: | High mobility group (HMG)-I proteins bind preferentially to the minor groove of A.T-rich regions in double-stranded DNA [, ]. DNA-binding of these, andseveral related, proteins is effected by an 11-residue domain known as an A.T-hook [].Within known HMG-I proteins are found three highly conserved regions, closely related to the consensus sequence TPKRPRGRPKK []. A synthetic oligopeptide with this sequence specifically binds to substrate DNA in a manner reminiscent of intact HMG-I proteins. Structure predictions suggestthat the peptide has a secondary structure similar to the anti-tumour and anti-viral drugs netropsin and distamycin []. These ligands, which also preferentially bind to A.T-rich DNA, effectively compete with both the synthetic peptide and the HMG-I proteins for DNA binding []. The peptide also contains novel structural features such as apredicted Asx bend, or "hook", at its N terminus, and laterally-projecting cationic Arg/Lys "bristles", which may play a role in the binding of HMG-Iproteins []. The predicted peptide structure, the A.T-hook, is a previouslyundescribed DNA-binding motif [].This family represents A.T-hook-like proteins. | Short Name: | AT_hook-like |
