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The sorcin–annexin VII calcium‐dependent interaction requires the sorcin N‐terminal domain
Author(s) -
Verzili Daniela,
Zamparelli Carlotta,
Mattei Benedetta,
Noegel Angelika A.,
Chiancone Emilia
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01396-x
Subject(s) - annexin , chemistry , calcium binding protein , annexin a2 , calcium , biophysics , biochemistry , biology , apoptosis , organic chemistry
Surface plasmon resonance experiments show that at neutral pH the stability of the complex between sorcin and annexin VII (synexin) increases dramatically between 3 and 6 μM calcium; at the latter cation concentration the K D value is 0.63 μM. In turn, the lack of complex formation between the sorcin Ca 2+ binding domain (33–198) and synexin maps the annexin binding site to the N‐terminal region of the sorcin polypeptide chain. Annexin VII likewise employs the N‐terminal domain, more specifically the first 31 amino acids, to interact with sorcin [Brownawell, A.M. and Creutz, C.E. (1997) J. Biol. Chem. 272, 22182–22190]. The interaction may involve similar structural motifs in the two proteins, namely GGYY and GYGG in sorcin and GYPP in synexin.