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PLoS One. 2014 Sep 8;9(9):e107309. doi: 10.1371/journal.pone.0107309. eCollection 2014.

Structural insights into the recognition of phosphopeptide by the FHA domain of kanadaptin.

Author information

1
Joint Center for Structural Genomics, La Jolla, California, United States of America; Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California, United States of America.
2
Joint Center for Structural Genomics, La Jolla, California, United States of America; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
3
Protein Production Facility, Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.
4
Joint Center for Structural Genomics, La Jolla, California, United States of America; Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California, United States of America.
5
Joint Center for Structural Genomics, La Jolla, California, United States of America; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America; Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California, United States of America.

Abstract

Kanadaptin is a nuclear protein of unknown function that is widely expressed in mammalian tissues. The crystal structure of the forkhead-associated (FHA) domain of human kanadaptin was determined to 1.6 Å resolution. The structure reveals an asymmetric dimer in which one monomer is complexed with a phosphopeptide mimic derived from a peptide segment from the N-terminus of a symmetry-related molecule as well as a sulfate bound to the structurally conserved phosphothreonine recognition cleft. This structure provides insights into the molecular recognition features utilized by this family of proteins and represents the first evidence that kanadaptin is likely involved in a phosphorylation-mediated signaling pathway. These results will be of use for designing experiments to further probe the function of kanadaptin.

PMID:
25197798
PMCID:
PMC4157861
DOI:
10.1371/journal.pone.0107309
[Indexed for MEDLINE]
Free PMC Article

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