Hyaluronidase

From Proteopedia

Revision as of 08:50, 27 March 2016

spinqualitylabelsall models Hyaluronidase complex with hyaluronic acid disaccharide and dimethylarsinate, 1c82 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural highlights Function Hyaluronidase (HU) hydrolyzes complex carbohydrates such as hyaluronan which is part of the extracellular matrix. The hydrolysis increases tissue permeability[1]. Superposition of the EGF-like domain of hyaluronidase-1 (yellow) and the heparin-binding EGF-like growth factor (light blue). The three disulfide bonds of the EGF domains (highlighted red) exhibit the same pattern in the primary structure and are located in similar positions in the 3D structure. Hyaluronidase cleaves the β1,4-glycosidic bond of the glycosaminoglycan hyaluronan Relevance HU is used in medicine to speed drug delivery. Hyaluronic acid (HUA) is a popular dermal filler material. Structural highlights HU structure contains an N-terminal, linker and C-terminal domains. The active site is in a cleft in the N-terminal domain. Two HUA molecules are bound in the active site making contacts with some HU residues and multiple contacts with water molecules[2].

3D structures of hyaluronidase

Updated on 27-March-2016

Reference

Structure of human hyaluronidase-1, a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis., Chao KL, Muthukumar L, Herzberg O, Biochemistry. 2007 Jun 12;46(23):6911-20. Epub 2007 May 16. PMID:17503783

1. ↑ Chao KL, Muthukumar L, Herzberg O. Structure of human hyaluronidase-1, a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis. Biochemistry. 2007 Jun 12;46(23):6911-20. Epub 2007 May 16. PMID:17503783 doi:10.1021/bi700382g
2. ↑ Ponnuraj K, Jedrzejas MJ. Mechanism of hyaluronan binding and degradation: structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 A resolution. J Mol Biol. 2000 Jun 16;299(4):885-95. PMID:10843845 doi:10.1006/jmbi.2000.3817

Created with the participation of Osnat Herzberg, Eran Hodis, Joel L. Sussman, Jaime Prilusky.