Abstract:
:By sequence analysis we show that the U104 domain found in the UNC104 subfamily of kinesins is a forkhead homology-associated domain (FHA). A combination of limited proteolysis, mass spectroscopy, and physicochemical analysis define this domain as a genuine autonomously folding domain. Our data show that the FHA domain is shorter than previously reported since the C-terminal alpha-helix is not part of its minimum core. Key amino acids postulated to recognize phosphorylated residues are conserved. These data suggest that the kinesin FHA domains are functional domains involved in protein-protein interactions regulated by phosphorylation.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Westerholm-Parvinen A,Vernos I,Serrano Ldoi
10.1016/s0014-5793(00)02310-3keywords:
subject
Has Abstractpub_date
2000-12-15 00:00:00pages
285-90issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(00)02310-3journal_volume
486pub_type
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