1NUE

X-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTION

Summary for 1NUE

• Entry DOI: 10.2210/pdb1nue/pdb
• Descriptor: NUCLEOSIDE DIPHOSPHATE KINASE, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: nucleoside triphosphate, nucleoside diphosphate, phosphotransferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P22392
• Total number of polymer chains: 6
• Total formula weight: 105864.97

Authors

Morera, S.,Lacombe, M.-L.,Yingwu, X.,Lebras, G.,Janin, J. (deposition date: 1995-10-06, release date: 1996-04-03, Last modification date: 2024-02-14)

Primary citation

Morera, S.,Lacombe, M.L.,Xu, Y.,LeBras, G.,Janin, J.
X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution.
Structure, 3:1307-1314, 1995

PubMed Abstract: Nucleoside diphosphate (NDP) kinases provide precursors for DNA and RNA synthesis. In mammals, these enzymes are also involved in cell regulations. Human NDP kinase B, product of the human nm23-H2 gene, is both an enzyme and a transcription factor. It activates transcription of the c-myc oncogene independently of its catalytic function, by binding to its promoter DNA. How do the two functions coexist?

PubMed: 8747457
DOI: 10.1016/S0969-2126(01)00268-4

Experimental method

X-RAY DIFFRACTION (2 Å)