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SUMMARY:Structure and function studies on  human plasminogen glycoforms
DTSTART;VALUE=DATE-TIME:20141120T011000Z
DTEND;VALUE=DATE-TIME:20141120T013000Z
DTSTAMP;VALUE=DATE-TIME:20260419T090430Z
UID:indico-contribution-678@events01.synchrotron.org.au
DESCRIPTION:Speakers: Ruby Law (Monash University)\nPlasminogen is a 7-dom
 ain protein (with an N-terminal Pan-apple domain\, five kringle domains an
 d a C-terminal serine protease domain) that adopts a closed\, activation-r
 esistant conformation in the circulatory system. The recruitment of plasmi
 nogen to its target sites is dependant on the lysine binding sites of the 
 kringle domains. Binding to lysine residues on cell receptors and fibrin c
 lots simultaneously triggers a conformational re-arrangement of the molecu
 le to adopt an open conformation. The open form is readily converted to pl
 asmin by tissue- and urokinase-type Plasminogen Activators. Plasmin plays 
 a key role in number of physiological and pathological processes including
  degradation of extracellular matrices\, cell migration\, tissue remodelin
 g\, wound healing\, angiogenesis\, inflammation\, pathogen invasion and ca
 ncer migration. \n\nWe have solved the X-ray crystal structure of human pl
 asminogen in the closed conformation. Our results revealed that the N-term
 inal Pan-apple domain and the serine protease domain maintain the closed c
 onformation via interactions made throughout the kringle array\, in partic
 ular\, Kringles 2\, 4 and 5. Our data suggests that Kringle 1 governs proe
 nzyme recruitment to target sites and binding to external lysine of Kringl
 e 5 in the closed conformation may trigger the formation of the open confo
 rmation. \n\nGlycosylation affects the overall conformation of the protein
  and therefore its functions. There are two plasminogen glycoforms in the 
 plasma\; our structural data suggests that these glycoforms have distinct 
 structural characteristics. Here we discuss our studies on the activation 
 and inhibition of these two glycoforms.\n\nhttps://events01.synchrotron.or
 g.au/event/3/contributions/678/
LOCATION: Oliphant Auditorium
URL:https://events01.synchrotron.org.au/event/3/contributions/678/
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