1fwo
From Proteopedia
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THE SOLUTION STRUCTURE OF A 35-RESIDUE FRAGMENT FROM THE GRANULIN/EPITHELIN-LIKE SUBDOMAIN OF RICE ORYZAIN BETA (ROB 382-416 (C398S,C399S,C407S,C413S))
Overview
A 35 amino acid residue peptide corresponding to the N-terminal subdomain, of the granulin-like repeat from rice oryzain beta was synthesized and, regioselectively oxidized to produce a species with a [1-3, 2-4], disulfide-pairing pattern. The resulting peptide was studied in solution, using NMR and was shown to adopt the tertiary topology of a stack of two, beta-hairpins found in the emerging family of granulin-like growth, factors. Because of the longer second beta-hairpin, the overall, conformation of the peptide is somewhat more flexible than that of its, well-structured carp granulin-1 analog. Except for the cysteine alignment, there is very little sequence homology between granulin-like growth, factors from the animal kingdom and the granulin-like repeats at the, C-termini of plant cysteine proteases. Therefore, the stack of two, beta-hairpins may be a conserved three-dimensional organization of the, granulin-like repeats from evolutionary distant sources with a significant, role in specific protein-protein interactions.
About this Structure
1FWO is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
A peptide derived from the C-terminal part of a plant cysteine protease folds into a stack of two beta-hairpins, a scaffold present in the emerging family of granulin-like growth factors., Tolkatchev D, Xu P, Ni F, J Pept Res. 2001 Mar;57(3):227-33. PMID:11298924
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