Engineering a calcium-dependent conformational change in Calbindin D9k by secondary elements replacement.
Arch Biochem Biophys
; 714: 109065, 2021 12 15.
Article
in En
| MEDLINE
| ID: mdl-34710387
EF-hand is a common motif in Ca2+-binding proteins, some of which present a conformational change upon Ca2+-binding, a relevant property for signal transduction. In the present work, we investigated the behavior of Calbindin D9k, a modulator protein with a high affinity for Ca2+ but structurally insensitive to its presence. Its non-canoncal N-terminal EF-hand was replaced by chimeric motifs, containing increasing structural elements from the sensor troponin C SCIII motif. We demonstrated that the loop and helix II were the necessary elements for a conformational change promoted by calcium in chimeric Calbindin D9k. Fusion of the isolated chimeric motifs to an activity reporter gene showed the loop as the minimal element to promote a conformational change. The discrepancy between these results is discussed in the light of inter-motif interactions and helix I participation in modulating the Ca2+ affinity and restricting motif conformation.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
S100 Calcium Binding Protein G
/
Calcium
Type of study:
Prognostic_studies
Language:
En
Journal:
Arch Biochem Biophys
Year:
2021
Document type:
Article
Affiliation country:
Mexico
Country of publication:
United States