Building kit for metal cation binding sites in proteins.

Alexandre Denesyuk, SE Permyakov, Mark S Johnson, EA Permyakov, Konstantin Denessiouk

Research output: Contribution to journalArticleScientificpeer-review

1 Citation (Scopus)

Abstract

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 Ca2+-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 "Ca2+-bound functional niches" in proteins revealed presence of almost all possible variants of Ca2+-recognition units in actual structures. Parvalbumin, integrin alpha-IIb and sixteen other proteins with different Ca2+-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: nitrogenn (Donor), oxygenn (Acceptor) and nitrogenn+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.

Original languageUndefined/Unknown
Pages (from-to)311–317
JournalBiochemical and Biophysical Research Communications
Volume494
Issue number1-2
DOIs
Publication statusPublished - 2017
MoE publication typeA1 Journal article-refereed

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