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Conformational and receptor binding properties of human EGF and TGF‐α second loop fragments
Author(s) -
Han KyouHoon,
Ferretti James A.,
Niu ChienHua,
Lokeshwar Vinatu,
Clarke Robert,
Katz Deborah
Publication year - 1988
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300010304
Subject(s) - homonuclear molecule , loop (graph theory) , chemistry , stereochemistry , receptor , nuclear overhauser effect , turn (biochemistry) , conformational change , peptide , fragment (logic) , nuclear magnetic resonance spectroscopy , biophysics , crystallography , molecule , biology , biochemistry , mathematics , organic chemistry , algorithm , combinatorics
The solution conformation of the second loop fragment of human EGF, [Ala 20 ]EGF(14–31), was determined using two‐dimensional NMR homonuclear Hartmann–Hahn and rotating frame nuclear Overhauser enhancement spectroscopy. The results are compared with the conformation of the second loop fragment of human TGF‐α, [Ala 21 ] TGF‐α(16–32), and with that of the second loop of intact EGF. Comparison of the two experimentally determined structures of the second loop fragments shows significant differences in the turn regions of each peptide. For the EGF fragment, hydrophobic side chain groups protrude away from the ring, whereas for the TGF‐α fragment hydrophilic groups are directed away from the ring. Although these turn regions represent the putative receptor binding sites, neither second loop fragment binds to the EGF receptor. The biological activity is discussed in terms of the conformational differences found for the two second loop fragments.