3OFW

Crystal structure of recombinant Kunitz Type serine protease Inhibitor-1 from the Carribean sea anemone stichodactyla helianthus

3OFW の概要

• エントリーDOI: 10.2210/pdb3ofw/pdb
• 関連するPDBエントリー: 3M7Q
• 分子名称: Kunitz-type proteinase inhibitor SHPI-1, CHLORIDE ION (3 entities in total)
• 機能のキーワード: kunitz type, serine protease inhibitor, serine protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Stichodactyla helianthus (Carribean sea anemone)
• 細胞内の位置: Secreted: P31713
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6730.86

構造登録者

Garcia-Fernandez, R.,Redecke, L.,Pons, T.,Perbandt, M.,Talavera, A.,Gil, D.,Gonzalez, Y.,de los Angeles Chavez, M.,Betzel, C. (登録日: 2010-08-16, 公開日: 2011-08-17, 最終更新日: 2024-11-20)

主引用文献

Garcia-Fernandez, R.,Pons, T.,Meyer, A.,Perbandt, M.,Gonzalez-Gonzalez, Y.,Gil, D.,de los Angeles Chavez, M.,Betzel, C.,Redecke, L.
Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus.
Acta Crystallogr.,Sect.F, 68:1289-1293, 2012

PubMed Abstract: The BPTI/Kunitz-type inhibitor family includes several extremely potent serine protease inhibitors. To date, the inhibitory mechanisms have only been studied for mammalian inhibitors. Here, the first crystal structure of a BPTI/Kunitz-type inhibitor from a marine invertebrate (rShPI-1A) is reported to 2.5 Å resolution. Crystallization of recombinant rShPI-1A required the salt-induced dissociation of a trypsin complex that was previously formed to avoid intrinsic inhibitor aggregates in solution. The rShPI-1A structure is similar to the NMR structure of the molecule purified from the natural source, but allowed the assignment of disulfide-bridge chiralities and the detection of an internal stabilizing water network. A structural comparison with other BPTI/Kunitz-type canonical inhibitors revealed unusual ϕ angles at positions 17 and 30 to be a particular characteristic of the family. A significant clustering of ϕ and ψ angle values in the glycine-rich remote fragment near the secondary binding loop was additionally identified, but its impact on the specificity of rShPI-1A and similar molecules requires further study.

PubMed: 23143234
DOI: 10.1107/S1744309112039085

実験手法

X-RAY DIFFRACTION (2.5 Å)