This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1fvu

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 09:03, 25 December 2014

CRYSTAL STRUCTURE OF BOTROCETIN

Structural highlights

1fvu is a 4 chain structure with sequence from Bothrops jararaca. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[BOTA_BOTJA] Snaclec that activates platelets by targeting vWF/GPIb. Two-chain botrocetin forms an activated complex with vWF (by binding the A1 domain), and the complex then binds to platelet glycoprotein Ibalpha (GP1BA), resulting in platelet aggregation. There are two distinct forms of the von Willebrand factor-dependent platelet coagglutinin. The dimeric form is 34-times more active than the one-chain botrocetin in promoting vWF binding to platelets. [BOTB_BOTJA] Snaclec that activates platelets by targeting vWF/GPIb. Two-chain botrocetin forms an activated complex with vWF (by binding the A1 domain), and the complex then binds to platelet glycoprotein Ibalpha (GP1BA), resulting in platelet aggregation. There are two distinct forms of the von Willebrand factor-dependent platelet coagglutinin. The dimeric form is 34-times more active than the one-chain botrocetin in promoting vWF binding to platelets.

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

The binding of von Willebrand factor (vWF) to the platelet receptor, glycoprotein (GP) Ib-IX-V complex, has a key role in the initiation of thrombus formation and is regulated by interactions with extracellular matrix components under the influence of hemodynamic forces. To a certain extent, these effects can be mimicked in vitro by two nonphysiologic modulators, ristocetin and botrocetin. The latter, isolated from the venom of the snake Bothrops jararaca, is a 31-kDa heterodimeric protein that forms a soluble complex with vWF. As an initial step toward understanding the mechanisms that regulate vWF function, we have solved the crystal structure of botrocetin at 1.8 A resolution. Botrocetin exhibits homology with other snake proteins, but contains only one metal binding site as compared to two in Factor IX binding protein and Factor IX/X binding protein and none in flavocetin. A distinctive feature of botrocetin is the presence of a negatively charged surface that may play a role in the association with the vWF A1 domain.

Crystal structure of the von Willebrand factor modulator botrocetin.,Sen U, Vasudevan S, Subbarao G, McClintock RA, Celikel R, Ruggeri ZM, Varughese KI Biochemistry. 2001 Jan 16;40(2):345-52. PMID:11148028^[1]

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

References

↑ Sen U, Vasudevan S, Subbarao G, McClintock RA, Celikel R, Ruggeri ZM, Varughese KI. Crystal structure of the von Willebrand factor modulator botrocetin. Biochemistry. 2001 Jan 16;40(2):345-52. PMID:11148028

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/1fvu"

@@ Line 6: / Line 6: @@
 <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=1fvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fvu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fvu RCSB], [http://www.ebi.ac.uk/pdbsum/1fvu PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/BOTA_BOTJA BOTA_BOTJA]] Snaclec that activates platelets by targeting vWF/GPIb. Two-chain botrocetin forms an activated complex with vWF (by binding the A1 domain), and the complex then binds to platelet glycoprotein Ibalpha (GP1BA), resulting in platelet aggregation. There are two distinct forms of the von Willebrand factor-dependent platelet coagglutinin. The dimeric form is 34-times more active than the one-chain botrocetin in promoting vWF binding to platelets. [[http://www.uniprot.org/uniprot/BOTB_BOTJA BOTB_BOTJA]] Snaclec that activates platelets by targeting vWF/GPIb. Two-chain botrocetin forms an activated complex with vWF (by binding the A1 domain), and the complex then binds to platelet glycoprotein Ibalpha (GP1BA), resulting in platelet aggregation. There are two distinct forms of the von Willebrand factor-dependent platelet coagglutinin. The dimeric form is 34-times more active than the one-chain botrocetin in promoting vWF binding to platelets.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1fvu

From Proteopedia

Revision as of 09:03, 25 December 2014

CRYSTAL STRUCTURE OF BOTROCETIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox