1gm2 | pdb_00001gm2

The independent structure of the antitryptic reactive site loop of Bowman-Birk inhibitor and sunflower trypsin inhibitor-1

spinqualitylabelsall models 1gm2 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gm2 is a 1 chain structure with sequence from Macrotyloma axillare. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 30 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function IBB4_MACAX Publication Abstract from PubMed 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 hydrogen bonding patterns in these inhibitors. The solution structure of the core peptide in isolation is found to retain essentially the same three-dimensional arrangement of both backbone and side chains as observed in larger antitryptic BBI and SFTI-1 fragments as well as in the complete proteins. The retention of the canonical conformation in the core peptide explains the peptids inhibitory potency. It therefore represents a minimization of both the BBI and SFTI-1 sequences. We conclude that the core peptide is a conformationally defined, canonical scaffold, which can serve as a minimal platform for the engineering of biological activity. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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