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1c3a

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Revision as of 07:42, 29 May 2019

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, 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] [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).^[3] ^[4]

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^[5]

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
↑ 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

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 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF FLAVOCETIN-A FROM THE HABU SNAKE VENOM, A NOVEL CYCLIC TETRAMER OF C-TYPE LECTIN-LIKE HETERODIMERS==
-<StructureSection load='1c3a' size='340' side='right' caption='[[1c3a]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<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>
@@ Line 12: / Line 12: @@
 Check<jmol>
   <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>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 31: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Trimeresurus flavoviridis]]
 [[Category: Atoda, H]]

1c3a

From Proteopedia

Revision as of 07:42, 29 May 2019

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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