PMID: 17503783

 

    Legend: Gene, Sites

Title : Structure of human hyaluronidase-1 , a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis

Abstract :

1. Mammalian hyaluronidases hydrolyze hyaluronan, a polysaccharide of diverse physiological roles found in all tissues and body fluids
2. In addition to its function in normal cellular hyaluronan turnover, human hyaluronidase-1 is implicated in cancer proliferation, angiogenesis, and inflammatory diseases; its expression is up-regulated in advanced stages of bladder cancer, whereas the expression of the alternative splice-variants is down-regulated
3. The crystal structure reveals a molecule composed of two closely associated domains : a catalytic domain that adopts a distorted (beta/alpha)8 barrel resembling that of bee venom hyaluronidase , and a novel, EGF-like domain , characteristic of involvement in protein-protein interactions and regulatory processes
4. The structure shows that the fold of this unique EGF-like domain is intact in four alternative splice-variants , whereas the catalytic domain is likely to be unfolded
5. Thus, these variants may function by competing with the full-length enzyme for the putative protein partner and regulating enzymatic activity in healthy cells

Output (sent_index, trigger, protein, sugar, site):

Output(Part-Of) (sent_index, protein, site):

• 3. EGF, domain
• 3. EGF, domains
• 4. EGF, domain

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX
hyaluronidase-1	3373	0,2