1LGP

Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein complexed with tungstate

Summary for 1LGP

• Entry DOI: 10.2210/pdb1lgp/pdb
• Related: 1LGQ
• Descriptor: cell cycle checkpoint protein CHFR, TUNGSTATE(VI)ION (3 entities in total)
• Functional Keywords: chfr, fha, tungstate, domain swapping, checkpoint, cell cycle
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus, PML body : Q96EP1
• Total number of polymer chains: 1
• Total formula weight: 13450.92

Authors

Stavridi, E.S.,Huyen, Y.,Loreto, I.R.,Scolnick, D.M.,Halazonetis, T.D.,Pavletich, N.P.,Jeffrey, P.D. (deposition date: 2002-04-16, release date: 2002-05-08, Last modification date: 2024-05-22)

Primary citation

Stavridi, E.S.,Huyen, Y.,Loreto, I.R.,Scolnick, D.M.,Halazonetis, T.D.,Pavletich, N.P.,Jeffrey, P.D.
Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate.
Structure, 10:891-899, 2002

PubMed Abstract: The Chfr mitotic checkpoint protein is frequently inactivated in human cancer. We determined the three-dimensional structure of its FHA domain in its native form and in complex with tungstate, an analog of phosphate. The structures revealed a beta sandwich fold similar to the previously determined folds of the Rad53 N- and C-terminal FHA domains, except that the Rad53 domains were monomeric, whereas the Chfr FHA domain crystallized as a segment-swapped dimer. The ability of the Chfr FHA domain to recognize tungstate suggests that it shares the ability with other FHA domains to bind phosphoproteins. Nevertheless, differences in the sequence and structure of the Chfr and Rad53 FHA domains suggest that FHA domains can be divided into families with distinct binding properties.

PubMed: 12121644
DOI: 10.1016/S0969-2126(02)00776-1

Experimental method

X-RAY DIFFRACTION (2 Å)