3ubu
From Proteopedia
Crystal structure of agkisacucetin, a GpIb-binding snaclec (snake C-type lectin) that inhibits platelet
Structural highlights
FunctionSLA1_DEIAC Agglucetin specifically causes platelet aggregation and surface exposure of integrin alpha-IIb/beta-3 with a GPIb-(GP1BA-) dependent manner in washed platelets. It binds to human platelets in a saturable manner, and its binding is specifically blocked by anti-GP Ib mAb. It regulates endothelial cell survival and promotes angiogenesis by activating integrin alpha-v/beta-3 signaling through FAK/phosphatidylinositol 3-kinase (PI3K)/Akt pathway.[1] [2] Publication Abstract from PubMedAgkisacucetin is a snake C-type lectin isolated from the venom of Agkistrodon acutus (A. acutus). It binds specifically to the platelet glycoprotein (GP) Ib and prevents the von Willebrand factor (VWF) accessing it. We determined the crystal structure of agkisacucetin to 1.9A resolution. The structure of agkisacucetin has an (alphabeta) fold similar to another GPIb-binding protein, flavocetin-A, but lacks the C-terminal cysteine in the beta-subunit, does not form (betaalpha)(4) tetramers, and does not cluster GPIbs, like flavocetin-A. Crystal structure of agkisacucetin, a Gpib-binding snake C-type lectin that inhibits platelet adhesion and aggregation.,Gao Y, Ge H, Chen H, Li H, Liu Y, Chen L, Li X, Liu J, Niu L, Teng M Proteins. 2012 Jun;80(6):1707-11. doi: 10.1002/prot.24060. Epub 2012 Mar 23. PMID:22447656[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Deinagkistrodon acutus | Large Structures | Chen H | Gao Y | Ge H | Li H | Liu Y | Niu L | Teng M
