Abstract:
:Annexins are multifunctional intracellular proteins with Ca2+- and phospholipid-binding properties. Their structures consist of four conserved repeat domains that form the core and a diverse N-terminal tail, from which their functional differences may arise. We searched for cellular proteins that interact with the N-terminal tail plus domain I of annexin I (ANX1) by using the yeast two-hybrid method. Screening of a HeLa cell cDNA library yielded annexin II (ANX2) cDNA. The interaction between ANX1 and ANX2 also occurred in vitro in a Ca2+-dependent manner. Mapping of the interaction sites revealed that interaction between domain I of ANX1 and domain IV of ANX2 was stronger than the other combinations.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Lee KH,Na DS,Kim JWdoi
10.1016/s0014-5793(98)01643-3subject
Has Abstractpub_date
1999-01-15 00:00:00pages
143-6issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01643-3journal_volume
442pub_type
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