Solution structure of the sequence-specific HMG box of the lymphocyte transcriptional activator Sox-4

Leo P.A. Van Houte, Vasily P. Chuprina, Marc Van Der Wetering, Rolf Boelens, Robert Kaptein, Hans Clevers

Research output: Contribution to journalArticlepeer-review

63 Citations (Scopus)

Abstract

Two groups of HMG box proteins are distinguished. Proteins in the first group contain multiple HMG boxes, are non-sequence-specific, and recognize structural features as found in cruciform DNA and cross-over DNA. The abundant chromosomal protein HMG-1 belongs to this subgroup. Proteins in the second group carry a single HMG box with affinity for the minor groove of the heptamer motif AACAAAG or variations thereof. A solution structure for the non-sequence-specific C-terminal HMG box of HMG-1 has recently been proposed. Now, we report the solution structure of the sequence-specific HMG-box of the SRY-related protein Sox-4. NMR analysis demonstrated the presence of three α-helices (Val10-Gln22, Glu30-Leu41 and Phe50-Tyr65) connected by loop regions (Ser23-Ala49 and Leu42-Pro49). Helices I and II are positioned in an antiparallel mode and form one arm of the HMG box. Helix III is less rigid, makes an average angle of about 90° with helices I and II, and constitutes the other arm of the molecule. As in HMG1B, the overall structure of the Sox-4 HMG box is L-shaped and is maintained by a cluster of conserved, mainly aromatic residues.

Original languageEnglish
Pages (from-to)30516-30524
Number of pages9
JournalJournal of Biological Chemistry
Volume270
Issue number51
DOIs
Publication statusPublished - 22 Dec 1995
Externally publishedYes

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