1GM2
The independent structure of the antitryptic reactive site loop of Bowman-Birk inhibitor and sunflower trypsin inhibitor-1
Summary for 1GM2
| Entry DOI | 10.2210/pdb1gm2/pdb |
| Descriptor | BOWMAN-BIRK INHIBITOR DERIVED PEPTIDE (1 entity in total) |
| Functional Keywords | bowman-birk inhibitor protein mimetic, sunflower trypsin inhibitor-1 (sfti-1) mimetic, trypsin inhibitor, type vib beta-turn peptide, hydrolase inhibitor |
| Biological source | Macrotyloma axillare |
| Total number of polymer chains | 1 |
| Total formula weight | 1227.43 |
| Authors | Brauer, A.B.E.,Kelly, G.,Matthews, S.J.,Leatherbarrow, R.J. (deposition date: 2001-09-08, release date: 2002-08-29, Last modification date: 2024-10-16) |
| Primary citation | Brauer, A.B.,Kelly, G.,Matthews, S.J.,Leatherbarrow, R.J. The (1)H-NMR solution structure of the antitryptic core peptide of Bowman-Birk inhibitor proteins: a minimal canonical loop. J.Biomol.Struct.Dyn., 20:59-70, 2002 Cited by PubMed Abstract: 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. PubMed: 12144352DOI: 10.1080/07391102.2002.10506822 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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