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1c3a

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Revision as of 18:01, 25 December 2014

CRYSTAL STRUCTURE OF FLAVOCETIN-A FROM THE HABU SNAKE VENOM, A NOVEL CYCLIC TETRAMER OF C-TYPE LECTIN-LIKE HETERODIMERS

Structural highlights

1c3a is a 2 chain structure with sequence from Trimeresurus flavoviridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[FLOA_PROFL] Strong platelet aggregation inhibitor. Binds specifically to platelet glycoprotein Ibalpha (GP1BA) with high affinity and inhibits vWF-dependent platelet aggregation (PubMed:7599152). Has also been observed to induce small agglutinates in washed platelets by binding to GPIb (PubMed:10688335).^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Crystal structure of flavocetin-A, a platelet glycoprotein Ib-binding protein, reveals a novel cyclic tetramer of C-type lectin-like heterodimers.,Fukuda K, Mizuno H, Atoda H, Morita T Biochemistry. 2000 Feb 29;39(8):1915-23. PMID:10684640^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Taniuchi Y, Kawasaki T, Fujimura Y, Suzuki M, Titani K, Sakai Y, Kaku S, Hisamichi N, Satoh N, Takenaka T, et al.. Flavocetin-A and -B, two high molecular mass glycoprotein Ib binding proteins with high affinity purified from Trimeresurus flavoviridis venom, inhibit platelet aggregation at high shear stress. Biochim Biophys Acta. 1995 Jun 9;1244(2-3):331-8. PMID:7599152
↑ Taniuchi Y, Kawasaki T, Fujimura Y. The high molecular mass, glycoprotein Ib-binding protein flavocetin-A induces only small platelet aggregates in vitro. Thromb Res. 2000 Jan 15;97(2):69-75. PMID:10688335
↑ 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. 2000 Feb 29;39(8):1915-23. PMID:10684640

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c3a"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c3a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c3a RCSB], [http://www.ebi.ac.uk/pdbsum/1c3a PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/FLOA_PROFL FLOA_PROFL]] Strong platelet aggregation inhibitor. Binds specifically to platelet glycoprotein Ibalpha (GP1BA) with high affinity and inhibits vWF-dependent platelet aggregation (PubMed:7599152). Has also been observed to induce small agglutinates in washed platelets by binding to GPIb (PubMed:10688335).<ref>PMID:7599152</ref> <ref>PMID:10688335</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1c3a

From Proteopedia

Revision as of 18:01, 25 December 2014

CRYSTAL STRUCTURE OF FLAVOCETIN-A FROM THE HABU SNAKE VENOM, A NOVEL CYCLIC TETRAMER OF C-TYPE LECTIN-LIKE HETERODIMERS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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