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3BSQ

Crystal structure of human kallikrein 7 produced as a secretion protein in E.coli

Summary for 3BSQ
Entry DOI10.2210/pdb3bsq/pdb
DescriptorKallikrein-7, SULFATE ION (3 entities in total)
Functional Keywordsserine proteases, kallikreins, ld6, x-ray crystal structure, glycoprotein, hydrolase, secreted, zymogen
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P49862
Total number of polymer chains3
Total formula weight76193.57
Authors
Fernandez, I.S.,Standker, L.,Magert, H.J.,Forssmann, W.G.,Gimenez-Gallego, G.,Romero, A. (deposition date: 2007-12-26, release date: 2008-04-29, Last modification date: 2024-11-13)
Primary citationFernandez, I.S.,Standker, L.,Magert, H.J.,Forssmann, W.G.,Gimenez-Gallego, G.,Romero, A.
Crystal structure of human epidermal kallikrein 7 (hK7) synthesized directly in its native state in E. coli: insights into the atomic basis of its inhibition by LEKTI domain 6 (LD6)
J.Mol.Biol., 377:1488-1497, 2008
Cited by
PubMed Abstract: Human kallikrein 7, a major protease of human skin, has been synthesized directly in its native conformation in Escherichia coli by forcing the secretion of the newly synthesized polypeptide into the bacterial periplasm. The procedure yields a stable kallikrein 7 with highly specific activity that is inhibited efficiently by its specific inhibitor LEKTI domain 6. The protein was crystallized, and its three-dimensional structure was solved in the absence of protease inhibitors. The structure obtained agrees with that reported recently for human tissue kallikrein 7 crystallized in the presence of protease inhibitors from a preparation obtained in a baculovirus protein expression system. A model of the interaction between the protease and its inhibitor is proposed on the basis of both the three-dimensional structure of human tissue kallikrein 7 reported here and that of the LEKTI domain 6 solved previously by NMR.
PubMed: 18329042
DOI: 10.1016/j.jmb.2008.01.089
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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