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Selection of novel structural zinc sites from a random peptide library
Author(s) -
Matsubara Teruhiko,
Hiura Yuko,
Kawahito Osamu,
Yasuzawa Mikito,
Kawashiro Katsuhiro
Publication year - 2003
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(03)01266-3
Subject(s) - zinc , dodecameric protein , peptide , chemistry , peptide library , circular dichroism , zinc finger , phage display , binding site , peptide sequence , active site , enzyme , biochemistry , stereochemistry , crystallography , dna , organic chemistry , gene , transcription factor
Zinc ion (Zn 2+ ) can be coordinated with four or three amino acid residues to stabilize a protein's structure or to form a catalytic active center. We used phage display selection of a dodecamer random peptide library with Zn 2+ to identify structural zinc sites. The binding specificity for Zn 2+ of selected sequences was confirmed using enzyme‐linked immunosorbent and competitive inhibition assays. Circular dichroism spectra indicated that the interaction with Zn 2+ induced a change in conformation, which means the peptide acts as a structural zinc site. Furthermore, a search of protein databases revealed that two selected sequences corresponded to parts of natural zinc sites of copper/zinc superoxide dismutase and zinc‐containing ferredoxin. We demonstrated that Zn 2+ ‐binding sequences selected from the random combinatorial library would be candidates for artificial structural zinc sites.