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Previously, we reported four point mutations in TLL1 found in approximately 20% of ASD6 patients. Three mutations in the coding sequence were M182L, V238A, and I629V. In this work, we present the effects of these mutations on TLL1 function. Three recombinant cDNA constructs carrying the mutations and one wild-type construct were prepared and then expressed in HT-1080 cells. Corresponding recombinant proteins were analyzed for their metalloendopeptidase activity using a native substrate, chordin. The results of these assays demonstrated that in comparison with the native TLL1, mutants cleaved chordin and procollagen I at significantly lower rates. CD analyses revealed significant structural differences between the higher order structure of wild-type and mutant variants. Moreover, biosensor-based assays of binding interactions between TLL1 variants and chordin demonstrated a significant decrease in the binding affinities of the mutated variants. The results from this work indicate that mutations detected in TLL1 of ASD6 patients altered its metalloendopeptidase activity, structure, and substrate-binding properties, thereby suggesting a possible pathomechanism of ASD6.<\/jats:p>","DOI":"10.1042\/bsr20180270","type":"journal-article","created":{"date-parts":[[2018,12,11]],"date-time":"2018-12-11T17:10:32Z","timestamp":1544548232000},"update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Functional and structural studies of tolloid-like 1 mutants associated with atrial-septal defect 6"],"prefix":"10.1042","volume":"39","author":[{"given":"Lukasz","family":"Sieron","sequence":"first","affiliation":[{"name":"Department of Molecular Biology and Genetics, School of Medicine in Katowice, Medical University of Silesia in Katowice, Katowice, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marta","family":"Lesiak","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Genetics, School of Medicine in Katowice, Medical University of Silesia in Katowice, Katowice, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Izabela","family":"Schisler","sequence":"additional","affiliation":[{"name":"Department of Medical Physics, Institute of Physics, University of Silesia, The Silesian Centre for Education and Interdisciplinary Research, Chorz\u00f3w, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zofia","family":"Drzazga","sequence":"additional","affiliation":[{"name":"Department of Medical Physics, Institute of Physics, University of Silesia, The Silesian Centre for Education and Interdisciplinary Research, Chorz\u00f3w, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrzej","family":"Fertala","sequence":"additional","affiliation":[{"name":"Department of Orthopedic Surgery, Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia, PA, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aleksander\u00a0L.","family":"Sieron","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Genetics, School of Medicine in Katowice, Medical University of Silesia in Katowice, Katowice, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2019,1,8]]},"reference":[{"key":"2021111617015939800_B1","doi-asserted-by":"publisher","first-page":"41905","DOI":"10.1074\/jbc.R111.299768","article-title":"Metalloproteinases in Drosophila to humans that are central players in developmental processes","volume":"286","author":"Muir","year":"2011","journal-title":"J. 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