Hyaluronidase: Difference between revisions

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</StructureSection>
</StructureSection>
==3D structures of hyaluronidase==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*Hyaluronidase
**[[2pe4]] – HU-1 – human<br />
**[[1fcq]], [[1fcu]] – bHU – bee<br />
**[[1egu]], [[2brw]] – SpHU – ''Streptococcus pneumoniae'' <br />
**[[4d0q]] – SpHU HUA binding domain<br />
**[[1n7n]], [[1n7o]], [[1n7p]] – SpHU (mutant) <br />
**[[1f1s]] – SaHU – ''Streptococcus agalactiae'' <br />
**[[2c3f]], [[2dp5]], [[2yw0]], [[2yx2]], [[2wb3]], [[2wh7]] - SpyHU – ''Streptococcus pyogenes''<br />
**[[2cbi]], [[2w1q]], [[2w1s]] - CpHU – ''Clostridium perfringens''<br />
**[[2jnk]] - CpHU residues 1498-1628]] - NMR<br />
**[[2atm]] - HU – ''Vespula vulgaris''<br />
**[[4ufq]] – HU – ''Streptomyces koganeiensis''<br />
*Hyaluronidase binary complex
**[[1fcv]] - bHU + HUA<br />
**[[2j88]] - bHU + FAB<br />
**[[1c82]] – SpHU + HUA disaccharide <br />
**[[1f9g]] – SpHU + ascorbate <br />
**[[2brv]]– SpHU + malonate<br />
**[[1loh]], [[1lxk]] - SpHU + glucuronic acid<br />
**[[1n7q]], [[1n7r]] - SpHU (mutant) + glucuronic acid<br />
**[[1ojm]], [[1ojp]] - SpHU + condroitin disaccharide <br />
**[[1ojn]], [[1ojo]] - SpHU (mutant) + condroitin disaccharide <br />
**[[1w3y]] - SpHU + palmitoyl-vitamin C <br />
**[[2brp]] – SpHU + inhibitor<br />
**[[1i8q]] - SaHU + HUA disaccharide <br />
**[[1lxm]] - SaHU + glucuronic acid<br />
**[[2cbj]] - CpHU + PugNac<br />
**[[2j1a]] - CpHU + galactose<br />
**[[2j1e]] - CpHU + LacNac<br />
**[[2j7m]], [[2w1u]], [[2wdb]] - CpHU + carbohydrates<br />
**[[2j62]] - CpHU + GlcNac-statin<br />
**[[2yvv]] - SpyHU + lactose<br />
**[[3eka]] - SpyHU + ascorbate <br />
**[[5diy]] – HU + Map3K 7 interacting protein peptide – ''Thermobaculum terrenum''<br />
}}


==Reference==
==Reference==
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<br />
<br />
Created with the participation of [[User:Osnat Herzberg|Osnat Herzberg]], [[User:Eran Hodis|Eran Hodis]], [[User:Joel L. Sussman|Joel L. Sussman]], [[User:Jaime Prilusky|Jaime Prilusky]].
Created with the participation of [[User:Osnat Herzberg|Osnat Herzberg]], [[User:Eran Hodis|Eran Hodis]], [[User:Joel L. Sussman|Joel L. Sussman]], [[User:Jaime Prilusky|Jaime Prilusky]].
    
    
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 13:21, 21 August 2019

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 disulphide 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 . 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].

. Water molecules are shown as red spheres.

.

.

3D structures of hyaluronidase

Hyaluronidase 3D structures


Hyaluronidase complex with hyaluronic acid disaccharide and dimethylarsinate, 1c82

Drag the structure with the mouse to rotate

ReferenceReference

  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.

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Michal Harel, Alexander Berchansky, Joel L. Sussman
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