The solution structure of the wild-type A box of rat HMG1 has been determined by heteronuclear three-dimensional NMR and molecular modelling. This structure adopts a "L" shape structure globaly similar to that described for a mutant A box and other HMG boxes. However the wild-type A box contains two Cys residues which could form an intramolecular bridge in an oxidative environment. This should be into competition with a contribution of the thiol groups in the binding of HMG proteins to cisplatin-modified DNA.
Solution structure of the wild-type HMG1 a box by1H and15N NMR and molecular modelling / Ohyama, Y.; Sodano, P.; Locker, D.; Bianchi, M. E.; Leng, M.; Vovelle, F.; Ptak, M.. - In: PROTEIN AND PEPTIDE LETTERS. - ISSN 0929-8665. - 4:2(1997), pp. 107-114. [10.2174/092986650402221012164202]
Solution structure of the wild-type HMG1 a box by1H and15N NMR and molecular modelling
Bianchi M. E.;
1997-01-01
Abstract
The solution structure of the wild-type A box of rat HMG1 has been determined by heteronuclear three-dimensional NMR and molecular modelling. This structure adopts a "L" shape structure globaly similar to that described for a mutant A box and other HMG boxes. However the wild-type A box contains two Cys residues which could form an intramolecular bridge in an oxidative environment. This should be into competition with a contribution of the thiol groups in the binding of HMG proteins to cisplatin-modified DNA.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
