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Sequence-specific 1H-n.m.r. assignments and peptide backbone conformation in rat epidermal growth factor.

Authors
  • Mayo, K H1
  • Cavalli, R C
  • Peters, A R
  • Boelens, R
  • Kaptein, R
  • 1 Department of Chemistry, Temple University, Philadelphia, PA 19122.
Type
Published Article
Journal
The Biochemical journal
Publication Date
Jan 01, 1989
Volume
257
Issue
1
Pages
197–205
Identifiers
PMID: 2784052
Source
Medline
License
Unknown

Abstract

The solution conformation of rat epidermal growth factor (EGF) has been investigated by proton n.m.r. techniques. Two-dimensional proton n.m.r. experiments have allowed sequential resonance assignments to be made for most protons. On the basis of these assignments, two regions of anti-parallel beta-sheet structure have been derived from the n.m.r. data. A beta-sheet segment running from about V19 to V23 (capital letters refer to amino acids in the single-letter notation) is folded onto a beta-sheet segment running from R28 to N32 and joined by a chain reversal from E24 to D27. A second region involves a beta-turn from V34 to Y37, which starts a short beta-sheet up to G39, followed by a chain reversal up to Q43, which leads to folding of the C-terminal beta-sheet segment, i.e. H44-R45, running antiparallel to the short Y37 beta-sheet segment. The N-terminal segment up to G18 exists in a multiple bend conformation and is folded on to the V29-V23/R28-N32 beta-sheet such that Y10, Y13, Y22 and Y29 are proximal to each other. Structural comparison of rat, murine and human EGFs indicates a number of highly conserved structural features common to at least these species of EGF.

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