1c3a: Difference between revisions

Latest revision as of 06:28, 30 October 2024

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 Protobothrops flavoviridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='1c3a' size='340' side='right'caption='[[1c3a]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1c3a]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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'>[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://pdbe.org/1c3a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c3a RCSB], [http://www.ebi.ac.uk/pdbsum/1c3a PDBsum], [http://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]] 2.5&#8491;</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>
 == Function ==
-[[http://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>  [[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 13: / Line 14: @@
    <jmolCheckbox>
      <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>
    </jmolCheckbox>
@@ Line 32: / Line 33: @@
 </StructureSection>
 [[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]]

1c3a: Difference between revisions

Latest revision as of 06:28, 30 October 2024

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

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