1i11
From Proteopedia
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SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN, SOX-5 HMG BOX FROM MOUSE
Overview
The fold of the murine Sox-5 (mSox-5) HMG box in free solution has been, determined by multidimensional NMR using (15)N-labeled protein and has, been found to adopt the characteristic twisted L-shape made up of two, wings: the major wing comprising helix 1 (F10--F25) and helix 2, (N32--A43), the minor wing comprising helix 3 (P51--Y67) in weak, antiparallel association with the N-terminal extended segment. (15)N, relaxation measurements show considerable mobility (reduced order, parameter, S(2)) in the minor wing that increases toward the amino and, carboxy termini of the chain. The mobility of residues C-terminal to Q62, is significantly greater than the equivalent residues of, non-sequence-specific boxes, and these residues show a weaker association, with the extended N-terminal segment than in non-sequence boxes., Comparison with previously determined structures of HMG boxes both in free, solution and complexed with DNA shows close similarity in the packing of, the hydrophobic cores and the relative disposition of the three helices., Only in hSRY/DNA does the arrangement of aromatic sidechains differ, significantly from that of mSox-5, and only in rHMG1 box 1 bound to, cisplatinated DNA does helix 1 have no kink. Helix 3 in mSox-5 is, terminated by P68, a conserved residue in DNA sequence-specific HMG boxes, which results in the chain turning through approximately 90 degrees.
About this Structure
1I11 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Solution structure and backbone dynamics of the DNA-binding domain of mouse Sox-5., Cary PD, Read CM, Davis B, Driscoll PC, Crane-Robinson C, Protein Sci. 2001 Jan;10(1):83-98. PMID:11266597
Page seeded by OCA on Tue Nov 20 16:57:50 2007
