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-Structure paper
タイトル | Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations. |
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ジャーナル・号・ページ | Protein Sci., Vol. 18, Page 1081-1094, Year 2009 |
掲載日 | 2008年7月31日 (構造データの登録日) |
![]() | Spraggon, G. / Hornsby, M. / Shipway, A. / Tully, D.C. / Bursulaya, B. / Danahay, H. / Harris, J.L. / Lesley, S.A. |
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手法 | X線回折 |
解像度 | 1.3 - 2.8 Å |
構造データ | ![]() PDB-3e0n: ![]() PDB-3e1x: ![]() PDB-3fvf: ![]() PDB-3gyl: ![]() PDB-3gym: |
化合物 | ![]() ChemComp-SO4: ![]() ChemComp-GOL: ![]() ChemComp-HOH: ![]() ChemComp-1JZ: ![]() ChemComp-DMS: ![]() ChemComp-CA: |
由来 |
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![]() | HYDROLASE / PROSTASIN / PROTEASE / chloromethyl-ketone / Channel / ENaC / Cell membrane / Glycoprotein / Membrane / Secreted / Serine protease / Transmembrane / Zymogen / HCAP-1 / Channel Activating Protease / INHIBITOR / DIVALENT CATION / CHANNEL ACTIVATING / Disulfide bond / HYDROLASE/INHIBITOR / hCAP1 / Aprotinin / inhibition / Pharmaceutical / Protease inhibitor / Serine protease inhibitor / HYDROLASE-INHIBITOR COMPLEX |