Building kit for metal cation binding sites in proteins
- Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino 142290 (Russian Federation)
- Faculty of Science and Engineering, Åbo Akademi University, Turku 20500 (Finland)
Starting with conformations of calcium-binding sites in parvalbumin and integrin (representative structures of EF-hand and calcium blade zones, respectively) we introduce four new different local Ca{sup 2+}-recognition units in proteins: a one-residue unit type I (ORI); a three-residue unit type I (TRI); a one-residue unit type II (ORII) and a three-residue unit type II (TRII). Based on the amount and nature of variable atoms, the type I and II units theoretically can have four and twelve variants, respectively. Analysis of known “Ca{sup 2+}-bound functional niches” in proteins revealed presence of almost all possible variants of Ca{sup 2+}-recognition units in actual structures. Parvalbumin, integrin alpha-IIb and sixteen other proteins with different Ca{sup 2+}-bound functional niches contain various consecutively joined combinations of OR(I/II) and TR(I/II) units. Such a OR(I/II)+TR(I/II) joint unit forms a tripeptide, which uses three main-chain atoms for metal binding: nitrogen{sub n} (Donor), oxygen{sub n} (Acceptor) and nitrogen{sub n+2} (Donor). Thus, taken together, the described ORI, TRI, ORII and TRII units can serve as elementary blocks to construct more complex calcium recognizing substructures in a variety of calcium binding sites of unrelated proteins.
- OSTI ID:
- 22719154
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 494, Issue 1-2; Other Information: Copyright (c) 2017 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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