Figure 4 - full size

 

Figure 4.
Figure 4. Comparison of DNA recognition modes between hTRF1 and hTRF2. (A) DNA recognition of the DNA-binding domain of hTRF2. The red circle indicates hydrophobic contact containing methyl groups of Ala484, Val485, and T3. Black broken lines indicate hydrophilic contacts between Asp489 and C7', C8'. (B) The interaction modes of Ser404/Ser417, Ala471/Ala484, and the phosphate group of T3. Black broken lines indicate hydrophilic contacts. (C) The interaction modes in the minor groove of DNA. Sidechains of Arg380 of hTRF1 and Lys447 of hTRF2, and DNA are shown. In hTRF1, the average distances over 20 structures between NH1 of Arg380 and O2 of T9, NH2 of Arg380 and O2 of T9, NH1 of Arg380 and N3 of A6', and NH2 of Arg380 and N3 of A6' are shown. In hTRF2, the average distances over 20 structures between NZ of Lys447 and O2 of T9, and NZ of Lys447 and N3 of A6' are shown. (D) The number of hydrogen bonds in the determined structures of the hTRF1 complex and the hTRF2 complex, respectively. The criteria of the hydrogen bonds were set as N-H o o D (O or N): N o o D distance < 3.5 Å; N-H-D angle > 90°.

The above figure is reprinted by permission from the Protein Society: Protein Sci (2005, 14, 119-130) copyright 2005.