Diabetes-associated mutations in a beta -cell transcription factor destabilize an antiparallel "mini-zipper" in a dimerization interface -- Data Supplement - Supplemental Figure 5 -- Proceedings of the National Academy of Sciences

Supplementary material for Hua et al. (2000) Proc. Natl. Acad. Sci. USA 97 (5), 1999-2004.

Fig. 5.
Regions of nuclear Overhauser enhancement (NOE) spectroscopy spectrum of hepatic nuclear factor (HNF)-1a dimerization domain in D₂O (pD 6.6). Representative interprotomeric NOEs are shown in red, intraprotomeric helix-helix NOEs in green, and ambiguous NOEs in magenta. (A) Contacts between Ha (vertical axis; w 2) and aliphatic resonances (horizontal axis; w 1). Assignments: (a) 9 Ha -21' d CH₃; (b) 21 Ha -5' d CH₃; (c) 5 Ha -21' d CH₃; (d) 23 Ha -16 d CH₃; (e) 23 Ha -17 d CH₃; and (f) 22 Ha -17 d CH₃. Other assignments shown (e.g., V5, L12) refer to intraresidue Ha -methyl NOEs. Arrows indicate a -helix-related (i, i + 3) and (i, i + 4) NOEs. (B) Contacts between Ha (vertical axis; w 2) and W33 aromatic resonances (horizontal axis; w 1). The W33 assignments are shown at left and methyl assignments at top. Other assignment: (g) dimer-related 33 H2-17' d CH₃ (red). Blue crosspeaks at right involve the methyl groups of L13, L17, or both. W33-L13 is a possible contact within a protomer, but W33-L17 is not possible within a protomer. Although W33 is not native to the sequence of HNF-1a , its resonances provide a probe for long-range orientation of the dimer. The mixing time was 200 ms.