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Protein Mimicry: A New Dimension for Peptides as Lead Compounds?
Author(s) -
Reineke Ulrich,
SchneiderMergener Jens
Publication year - 1998
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19980403)37:6<769::aid-anie769>3.0.co;2-b
Subject(s) - mimicry , peptide , molecular mimicry , dimer , chemistry , receptor , phage display , biochemistry , peptide sequence , amino acid , biology , computational biology , antibody , genetics , ecology , organic chemistry , gene
A short peptide as mimic for the hemopoietic growth factor erythropoietin (containing 165 amino acids) could be identified with the aid of peptide libraries on phage surfaces (phage display). The crystal structure of a peptide dimer complexed with two erythropoietin receptors (shown on the right) provides an insight into the molecular basis of this protein mimicry.