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| | <StructureSection load='1c3a' size='340' side='right'caption='[[1c3a]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1c3a' size='340' side='right'caption='[[1c3a]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1c3a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trimeresurus_flavoviridis Trimeresurus flavoviridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C3A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1c3a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Protobothrops_flavoviridis Protobothrops flavoviridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C3A FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c3a OCA], [https://pdbe.org/1c3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c3a RCSB], [https://www.ebi.ac.uk/pdbsum/1c3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c3a ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c3a OCA], [https://pdbe.org/1c3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c3a RCSB], [https://www.ebi.ac.uk/pdbsum/1c3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c3a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SLAA_PROFL SLAA_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:10688335</ref> <ref>PMID:7599152</ref> [[https://www.uniprot.org/uniprot/SLAB_PROFL SLAB_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:10688335</ref> <ref>PMID:7599152</ref>
| + | [https://www.uniprot.org/uniprot/SLAA_PROFL SLAA_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:10688335</ref> <ref>PMID:7599152</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c3/1c3a_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c3/1c3a_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trimeresurus flavoviridis]] | + | [[Category: Protobothrops flavoviridis]] |
| - | [[Category: Atoda, H]] | + | [[Category: Atoda H]] |
| - | [[Category: Fukuda, K]] | + | [[Category: Fukuda K]] |
| - | [[Category: Mizuno, H]] | + | [[Category: Mizuno H]] |
| - | [[Category: Morita, T]] | + | [[Category: Morita T]] |
| - | [[Category: C-type lectin-like domain]]
| + | |
| - | [[Category: Membrane protein]]
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| Structural highlights
Function
SLAA_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. 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
- ↑ 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
- ↑ 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
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