1C3A
CRYSTAL STRUCTURE OF FLAVOCETIN-A FROM THE HABU SNAKE VENOM, A NOVEL CYCLIC TETRAMER OF C-TYPE LECTIN-LIKE HETERODIMERS
Summary for 1C3A
| Entry DOI | 10.2210/pdb1c3a/pdb |
| Descriptor | FLAVOCETIN-A: ALPHA SUBUNIT, FLAVOCETIN-A: BETA SUBUNIT (3 entities in total) |
| Functional Keywords | c-type lectin-like domains, membrane protein |
| Biological source | Trimeresurus flavoviridis More |
| Total number of polymer chains | 2 |
| Total formula weight | 30230.68 |
| Authors | Fukuda, K.,Mizuno, H.,Atoda, H.,Morita, T. (deposition date: 1999-07-27, release date: 2000-03-06, Last modification date: 2024-10-30) |
| Primary citation | Fukuda, K.,Mizuno, H.,Atoda, H.,Morita, T. Crystal structure of flavocetin-A, a platelet glycoprotein Ib-binding protein, reveals a novel cyclic tetramer of C-type lectin-like heterodimers. Biochemistry, 39:1915-1923, 2000 Cited by PubMed Abstract: Snake venom contains a number of the hemostatically active C-type lectin-like proteins, which affect the interaction between von Willebrand factor (vWF) and the platelet glycoprotein (GP) Ib or platelet receptor to inhibit/induce platelet activation. Flavocetin-A (FL-A) is a high-molecular mass C-type lectin-like protein (149 kDa) isolated from the habu snake venom. FL-A binds with high affinity to the platelet GP Ibalpha-subunit and functions as a strong inhibitor of vWF-dependent platelet aggregation. We have determined the X-ray crystal structure of FL-A and refined to 2.5 A resolution. This is a first elucidation of a three-dimensional structure of the platelet GP Ib-binding protein. The overall structure reveals that the molecule is a novel cyclic tetramer (alphabeta)(4) made up of four alphabeta-heterodimers related by a crystallographic 4-fold symmetry. The tetramerization is mediated by an interchain disulfide bridge between cysteine residues at the C-terminus of the alpha-subunit and at the N-terminus of the beta-subunit in the neighboring alphabeta-heterodimer. The high affinity of FL-A for the platelet GP Ib alpha-subunit could be explained by a cooperative-binding action through the multiple binding sites of the tetramer. PubMed: 10684640DOI: 10.1021/bi992134z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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