4doq | pdb_00004doq

Crystal structure of the complex of Porcine Pancreatic Trypsin with 1/2SLPI

spinqualitylabelsall models 4doq, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4doq is a 5 chain structure with sequence from Homo sapiens and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: CA, P6G, SO4, XPE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRYP_PIG Publication Abstract from PubMed SLPI (secretory leukocyte protease inhibitor) is a 107-residue protease inhibitor which inhibits various serine proteases, including elastase, cathepsin G, chymotrypsin and trypsin. SLPI is obtained as a multiple inhibitor in lung defense and in chronic airway infection. X-ray crystal structures have so far reported that they are full-length SLPIs with bovine alpha-chymotrypsin and 1/2SLPI (recombinant C-terminal domain of SLPI; Arg58-Ala107) with HNE (human neutrophil elastase). To understand the role of this multiple inhibitory mechanism, the crystal structure of 1/2SLPI with porcine pancreas trypsin was solved and the binding modes of two other complexes compared. The Leu residue surprisingly interacts with the S1 site of trypsin, as with chymotrypsin and elastase. The inhibitory mechanism of 1/2SLPI using the wide primary binding site contacts (from P2' to P5) with various serine proteases is discussed. These inhibitory mechanisms have been acquired in the evolution of the protection system for acute inflammatory diseases. Structure basis 1/2SLPI and porcine pancreas trypsin interaction.,Fukushima K, Kamimura T, Takimoto-Kamimura M J Synchrotron Radiat. 2013 Nov;20(Pt 6):943-7. doi: 10.1107/S090904951302133X., Epub 2013 Sep 29. PMID:24121345 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypsin 3D structures

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