1gm2
From Proteopedia
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THE INDEPENDENT STRUCTURE OF THE ANTITRYPTIC REACTIVE SITE LOOP OF BOWMAN-BIRK INHIBITOR AND SUNFLOWER TRYPSIN INHIBITOR-1
Overview
Bowman-Birk inhibitor (BBI) proteins contain an inhibitory motif, comprising a disulfide-bonded sequence that interacts with serine, proteinases. Recently, a small 14-residue peptide from sunflowers, (SFTI-1), which has potent anti-trypsin activity, has been found to have, the same motif. However, this peptide also has an unusual head-to-tail, cyclisation. To address the role of the core inhibitory sequence itself, we have solved the (1)H-NMR solution structure of an antitryptic, 11-residue cyclic peptide that corresponds to the core reactive site loops, of both SFTI-1 and Bowman-Birk inhibitor proteins. A comparison is made, between the secondary chemical shifts found in this family and the, canonical regions of several other inhibitors, giving some insight into, relative flexibility and ... [(full description)]
About this Structure
1GM2 is a [Single protein] structure of sequence from [[1]]. Structure known Active Site: P1. Full crystallographic information is available from [OCA].
Reference
The (1)H-NMR solution structure of the antitryptic core peptide of Bowman-Birk inhibitor proteins: a minimal canonical loop., Brauer AB, Kelly G, Matthews SJ, Leatherbarrow RJ, J Biomol Struct Dyn. 2002 Aug;20(1):59-70. PMID:12144352
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