Active site specificity profiling datasets of matrix metalloproteinases (MMPs) 1, 2, 3, 7, 8, 9, 12, 13 and 14

• Published in: Data in brief 2016-06, Vol.7, p.299-310
• Main Authors: Eckhard, Ulrich, Huesgen, Pitter F., Schilling, Oliver, Bellac, Caroline L., Butler, Georgina S., Cox, Jennifer H., Dufour, Antoine, Goebeler, Verena, Kappelhoff, Reinhild, auf dem Keller, Ulrich, Klein, Theo, Lange, Philipp F., Marino, Giada, Morrison, Charlotte J., Prudova, Anna, Rodriguez, David, Starr, Amanda E., Wang, Yili, Overall, Christopher M.
• Format: Article
• Language: English
• Subjects: Cleavage sites; Data; Matrix metalloproteinases; MMPs; PICS; Proteomics; Quenched fluorescence; Specificity profiling
• ISSN: 2352-3409; 2352-3409
• DOI: 10.1016/j.dib.2016.02.036

The data described provide a comprehensive resource for the family-wide active site specificity portrayal of the human matrix metalloproteinase family. We used the high-throughput proteomic technique PICS (Proteomic Identification of protease Cleavage Sites) to comprehensively assay 9 different MMPs. We identified more than 4300 peptide cleavage sites, spanning both the prime and non-prime sides of the scissile peptide bond allowing detailed subsite cooperativity analysis. The proteomic cleavage data were expanded by kinetic analysis using a set of 6 quenched-fluorescent peptide substrates designed using these results. These datasets represent one of the largest specificity profiling efforts with subsequent structural follow up for any protease family and put the spotlight on the specificity similarities and differences of the MMP family. A detailed analysis of this data may be found in Eckhard et al. (2015) [1]. The raw mass spectrometry data and the corresponding metadata have been deposited in PRIDE/ProteomeXchange with the accession number http://www.ebi.ac.uk/pride/archive/projects/PXD002265.