1HMA

THE SOLUTION STRUCTURE AND DYNAMICS OF THE DNA BINDING DOMAIN OF HMG-D FROM DROSOPHILA MELANOGASTER

Summary for 1HMA

• Entry DOI: 10.2210/pdb1hma/pdb
• Descriptor: HMG-D (1 entity in total)
• Functional Keywords: dna-binding
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Nucleus: Q05783
• Total number of polymer chains: 1
• Total formula weight: 8370.51

Authors

Jones, D.N.M.,Searles, M.A.,Shaw, G.L.,Churchill, M.E.A.,Ner, S.S.,Keeler, J.,Travers, A.A.,Neuhaus, D. (deposition date: 1994-05-12, release date: 1994-07-31, Last modification date: 2024-05-22)

Primary citation

Jones, D.N.,Searles, M.A.,Shaw, G.L.,Churchill, M.E.,Ner, S.S.,Keeler, J.,Travers, A.A.,Neuhaus, D.
The solution structure and dynamics of the DNA-binding domain of HMG-D from Drosophila melanogaster.
Structure, 2:609-627, 1994

PubMed Abstract: The HMG-box is a conserved DNA-binding motif that has been identified in many high mobility group (HMG) proteins. HMG-D is a non-histone chromosomal protein from Drosophila melanogaster that is closely related to the mammalian HMG-box proteins HMG-1 and HMG-2. Previous structures determined for an HMG-box domain from rat and hamster exhibit the same global topology, but differ significantly in detail. It has been suggested that these differences may arise from hinge motions which allow the protein to adapt to the shape of its target DNA.

PubMed: 7922039
DOI: 10.1016/S0969-2126(00)00063-0

Experimental method

SOLUTION NMR