| Literature DB >> 1761036 |
R M Cooke1, B G Carter, D M Martin, P Murray-Rust, M P Weir.
Abstract
The 1H-NMR spectrum of the snake toxin echistatin has been assigned using homonuclear two-dimensional methods. Consideration of the NOE patterns, coupling constants and putative hydrogen bonds enabled two regular features of secondary structure to be deduced: a beta-sheet/turn between residues 8 and 13 and a small anti-parallel beta-sheet and bulge linking residues 16-20 with residues 30-33. The recognition region of the protein containing the residues RGD lies in a loop joining the two strands of the beta-sheet. The beta-bulge and the loop containing the RGD sequence undergo pH-dependent conformational interconversion, modulated by the side chain of Asp29.Entities:
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Year: 1991 PMID： 1761036 DOI： 10.1111/j.1432-1033.1991.tb16379.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956