3UBU

Crystal structure of agkisacucetin, a GpIb-binding snaclec (snake C-type lectin) that inhibits platelet

Summary for 3UBU

• Entry DOI: 10.2210/pdb3ubu/pdb
• Descriptor: Agglucetin subunit alpha-1, Agglucetin subunit beta-2, SULFATE ION, ... (5 entities in total)
• Functional Keywords: platelet inhibiting, agkisacucetin, dimer, toxin, c-type lectin-like, gpib inhibitor, gpib binding
• Biological source: Deinagkistrodon acutus (Hundred-pace snake); More
• Cellular location: Secreted (By similarity): Q8JIV9 Q8AYA3
• Total number of polymer chains: 2
• Total formula weight: 30155.93

Authors

Gao, Y.,Ge, H.,Chen, H.,Li, H.,Liu, Y.,Niu, L.,Teng, M. (deposition date: 2011-10-25, release date: 2012-04-11, Last modification date: 2025-03-26)

Primary citation

Gao, Y.,Ge, H.,Chen, H.,Li, H.,Liu, Y.,Chen, L.,Li, X.,Liu, J.,Niu, L.,Teng, M.
Crystal structure of agkisacucetin, a Gpib-binding snake C-type lectin that inhibits platelet adhesion and aggregation.
Proteins, 2012

PubMed Abstract: Agkisacucetin 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 1.9Å resolution. The structure of agkisacucetin has an (αβ) fold similar to another GPIb-binding protein, flavocetin-A, but lacks the C-terminal cysteine in the β-subunit, does not form (βα)(4) tetramers, and does not cluster GPIbs, like flavocetin-A.

PubMed: 22447656
DOI: 10.1002/prot.24060

Experimental method

X-RAY DIFFRACTION (1.91 Å)