5ue5 | pdb_00005ue5

proMMP-7 with heparin octasaccharide bound to the catalytic domain

spinqualitylabelsall models 5ue5, 16 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ue5 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, IDS, SGN, ZN Related: 2mze, 5ue2 Gene: MMP7, MPSL1, PUMP1 (HUMAN) Activity: Matrilysin, with EC number 3.4.24.23 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MMP7_HUMAN] Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase. Publication Abstract from PubMed Heparan sulfate proteoglycans activate the matrix metalloproteinase-7 zymogen (proMMP-7) and recruit it in order to shed proteins from cell surfaces. This occurs in uterine and mammary epithelia, bacterial killing, lung healing, and tumor cell signaling. Basic tracks on proMMP-7 recognize polyanionic heparin, according to nuclear magnetic resonance and mutations disruptive of maturation. Contacts and proximity measurements guided docking of a heparin octasaccharide to proMMP-7. The reducing end fits into a basic pocket in the pro-domain while the chain continues toward the catalytic domain. Another oligosaccharide traverses a basic swath remote on the catalytic domain and inserts its reducing end into a slot formed with the basic C terminus. This latter association appears to support allosteric acceleration of proteolysis. The modes of binding account for extended, heterogeneous assemblies of proMMP-7 with heparinoids during maturation and for bridging to pro-alpha-defensins and proteoglycans. These associations support proteolytic release of activities at epithelial cell surfaces. Glycan Activation of a Sheddase: Electrostatic Recognition between Heparin and proMMP-7.,Fulcher YG, Prior SH, Masuko S, Li L, Pu D, Zhang F, Linhardt RJ, Van Doren SR Structure. 2017 Jul 5;25(7):1100-1110.e5. doi: 10.1016/j.str.2017.05.019. Epub, 2017 Jun 22. PMID:28648610 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Matrix metalloproteinase 3D structures

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