1lgp | pdb_00001lgp
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Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein complexed with tungstate
Overview
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.
About this Structure
1LGP is a Single protein structure of sequence from Homo sapiens with WO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate., Stavridi ES, Huyen Y, Loreto IR, Scolnick DM, Halazonetis TD, Pavletich NP, Jeffrey PD, Structure. 2002 Jul;10(7):891-9. PMID:12121644
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