SOLUTION STRUCTURE OF A FRAGMENT OF THE DIMERIZATION DOMAIN OF E2F-1 DETERMINED BY CIRCULAR-DICHROISM, H-1 NUCLEAR-MAGNETIC-RESONANCE AND DISTANCE GEOMETRY

The structure of a synthesized peptide with the sequence GVVDLNWAAEVLK VQKRRIYDITNVLEGIQ which corresponds to residues 149-178 of transcripti on factor E2F-1 was determined by H-1 nuclear magnetic resonance in 40 % d(3)-TFE/water. NOE cross peaks and alpha H chemical shifts indicate that the peptide consists of a helix from Ala-8 to Leu-26 in this sol ution. Circular dichroism measurements confirm the presence of nearly 45% helix in TFE/water solution but show no evidence of helicity in wa ter solution of this peptide. Fifty structures were constructed with 3 29 upper distance limits by DIANE. The 20 best conformers show a RMSD of 0.78 Angstrom for backbone atoms and 1.78 Angstrom for heavy atoms from residue Ala-8 to Leu-26. This result, together with our previous work on the solution structure of a fragment of DP-1, supports the pro posal that E2F-1 and DP-1 may dimerize with a coiled-coil type interac tion. (C) 1998 Elsevier Science B.V. All rights reserved.