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Instruments / Technical Area	Publication Details	Published	Actions
B21-High Throughput SAXS I02-Macromolecular Crystallography I03-Macromolecular Crystallography	Dynamics of the secreted frizzled related protein Sizzled and potential implications for binding to bone morphogenetic protein-1 (BMP-1) Urvashi Sharma , Sandrine Vadon-Le Goff , Karl Harlos , Yuguang Zhao , Natacha Mariano , Cecile Bijakowski , Jean-Marie Bourhis , Catherine Moali , David J. S. Hulmes , Nushin Aghajari Scientific Reports 12 DOI: 10.1038/s41598-022-18795-4 Diamond Proposal Number(s): [8423] Open Access Show Abstract ▼ Abstract: Sizzled (Szl) is both a secreted frizzled related protein (sFRP) and a naturally occurring inhibitor of the zinc metalloproteinase bone morphogenetic protein-1 (BMP-1), a key regulator of extracellular matrix assembly and growth factor activation. Here we present a new crystal structure for Szl which differs from that previously reported by a large scale (90°) hinge rotation between its cysteine-rich and netrin-like domains. We also present results of a molecular docking analysis showing interactions likely to be involved in the inhibition of BMP-1 activity by Szl. When compared with known structures of BMP-1 in complex with small molecule inhibitors, this reveals features that may be helpful in the design of new inhibitors to prevent the excessive accumulation of extracellular matrix that is the hallmark of fibrotic diseases.	Sep 2022
B21-High Throughput SAXS	Structural basis of homo- and heterotrimerization of collagen I Urvashi Sharma , Loïc Carrique , Sandrine Vadon-Le Goff , Natacha Mariano , Rainier-Numa Georges , Frederic Delolme , Peppi Koivunen , Johanna Myllyharju , Catherine Moali , Nushin Aghajari , David J. S. Hulmes Nature Communications 8 DOI: 10.1038/ncomms14671 Diamond Proposal Number(s): [9634] Open Access Show Abstract ▼ Abstract: Fibrillar collagen molecules are synthesized as precursors, procollagens, with large propeptide extensions. While a homotrimeric form (three α1 chains) has been reported in embryonic tissues as well as in diseases (cancer, fibrosis, genetic disorders), collagen type I usually occurs as a heterotrimer (two α1 chains and one α2 chain). Inside the cell, the role of the C-terminal propeptides is to gather together the correct combination of three α chains during molecular assembly, but how this occurs for different forms of the same collagen type is so far unknown. Here, by structural and mutagenic analysis, we identify key amino acid residues in the α1 and α2 C-propeptides that determine homo- and heterotrimerization. A naturally occurring mutation in one of these alters the homo/heterotrimer balance. These results show how the C-propeptide of the α2 chain has specifically evolved to permit the appearance of heterotrimeric collagen I, the major extracellular building block among the metazoa.	Mar 2017

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