Building kit for metal cation binding sites in proteins.

A1 Journal article (refereed)

Internal Authors/Editors

Publication Details

List of Authors: Denesyuk AI, Permyakov SE, Johnson MS, Permyakov EA, Denessiouk K.
Publisher: ELSEVIER
Publication year: 2017
Journal: Biochemical and Biophysical Research Communications
Journal acronym: BBRC
Volume number: 494
Issue number: 1-2
Start page: 311
End page: 317


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.

Last updated on 2019-16-10 at 03:15