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The mature part of proNGF induces the structure of its pro‐peptide
Author(s) -
Kliemannel Marco,
Rattenholl Anke,
Golbik Ralph,
Balbach Jochen,
Lilie Hauke,
Rudolph Rainer,
Schwarz Elisabeth
Publication year - 2004
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/j.febslet.2004.04.034
Subject(s) - peptide , chemistry , oxidative folding , protein folding , disulfide bond , cystine , biochemistry , protein structure , protein disulfide isomerase , enzyme , cysteine
Human nerve growth factor (NGF) belongs to the structural family of cystine knot proteins, characterized by a disulfide pattern in which one disulfide bond threads through a ring formed by a pair of two other disulfides connecting two adjacent β‐strands. Oxidative folding of NGF revealed that the pro‐peptide of NGF stimulates in vitro structure formation. In order to learn more about this folding assisting protein fragment, a biophysical analysis of the pro‐peptide structure has been performed. While proNGF is a non‐covalent homodimer, the isolated pro‐peptide is monomeric. No tertiary contacts stabilize the pro‐peptide in its isolated form. In contrast, the pro‐peptide appears to be structured when bound to the mature part. The results presented here demonstrate that the mature part stabilizes the structure in the pro‐peptide region. This is the first report that provides a biophysical analysis of a pro‐peptide of the cystine knot protein family.