Ontology highlight
ABSTRACT:
SUBMITTER: Cerdan R
PROVIDER: S-EPMC2374130 | biostudies-literature | 2001 Mar
REPOSITORIES: biostudies-literature
Cerdan R R Payet D D Yang J C JC Travers A A AA Neuhaus D D
Protein science : a publication of the Protein Society 20010301 3
An NMR model is presented for the structure of HMG-D, one of the Drosophila counterparts of mammalian HMG1/2 proteins, bound to a particular distorted DNA structure, a dA(2) DNA bulge. The complex is in fast to intermediate exchange on the NMR chemical shift time scale and suffers substantial linebroadening for the majority of interfacial resonances. This essentially precludes determination of a high-resolution structure for the interface based on NMR data alone. However, by introducing a small ...[more]