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3c05

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Revision as of 00:03, 10 February 2016

Crystal structure of Acostatin from Agkistrodon Contortrix Contortrix

Structural highlights

3c05 is a 4 chain structure with sequence from Agkistrodon contortrix contortrix. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[DIDA_AGKCO] Inhibits fibrinogen interaction with platelets. Acts by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and inhibits ADP-induced platelet aggregation in human platelet-rich plasma.^[1] [VM2AB_AGKCO] Snake venom metalloproteinase: impairs hemostasis in the envenomed animal (By similarity). This product has not been identified in the venom. Disintegrin acostatin-beta: inhibits platelet aggregation in human platelet-rich plasma induced by ADP. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3).

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

Disintegrins are a family of small (4-14 kDa) proteins that bind to another class of proteins, integrins. Therefore, as integrin inhibitors, they can be exploited as anticancer and antiplatelet agents. Acostatin, an alphabeta heterodimeric disintegrin, has been isolated from the venom of Southern copperhead (Agkistrodon contortrix contortrix). The three-dimensional structure of acostatin has been determined by macromolecular crystallography using the molecular-replacement method. The asymmetric unit of the acostatin crystals consists of two heterodimers. The structure has been refined to an R(work) and R(free) of 18.6% and 21.5%, respectively, using all data in the 20-1.7 A resolution range. The structure of all subunits is similar and is well ordered into N-terminal and C-terminal clusters with four intramolecular disulfide bonds. The overall fold consists of short beta-sheets, each of which is formed by a pair of antiparallel beta-strands connected by beta-turns and flexible loops of different lengths. Conformational flexibility is found in the RGD loops and in the C-terminal segment. The interaction of two N-terminal clusters via two intermolecular disulfide bridges anchors the alphabeta chains of the acostatin dimers. The C-terminal clusters of the heterodimer project in opposite directions and form a larger angle between them in comparison with other dimeric disintegrins. Extensive interactions are observed between two heterodimers, revealing an alphabetabetaalpha acostatin tetramer. Further experiments are required to identify whether the alphabetabetaalpha acostatin complex plays a functional role in vivo.

Structure of acostatin, a dimeric disintegrin from Southern copperhead (Agkistrodon contortrix contortrix), at 1.7 A resolution.,Moiseeva N, Bau R, Swenson SD, Markland FS Jr, Choe JY, Liu ZJ, Allaire M Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):466-70. Epub 2008, Mar 19. PMID:18391413^[2]

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

References

↑ Okuda D, Koike H, Morita T. A new gene structure of the disintegrin family: a subunit of dimeric disintegrin has a short coding region. Biochemistry. 2002 Dec 3;41(48):14248-54. PMID:12450389
↑ Moiseeva N, Bau R, Swenson SD, Markland FS Jr, Choe JY, Liu ZJ, Allaire M. Structure of acostatin, a dimeric disintegrin from Southern copperhead (Agkistrodon contortrix contortrix), at 1.7 A resolution. Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):466-70. Epub 2008, Mar 19. PMID:18391413 doi:10.1107/S0907444908002370

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3c05"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=3c05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c05 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c05 RCSB], [http://www.ebi.ac.uk/pdbsum/3c05 PDBsum]</span></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=3c05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c05 OCA], [http://pdbe.org/3c05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3c05 RCSB], [http://www.ebi.ac.uk/pdbsum/3c05 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DISA_AGKCO DISA_AGKCO]] Inhibits fibrinogen interaction with platelets. Acts by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and inhibits ADP-induced platelet aggregation in human platelet-rich plasma.<ref>PMID:12450389</ref>
+[[http://www.uniprot.org/uniprot/DIDA_AGKCO DIDA_AGKCO]] Inhibits fibrinogen interaction with platelets. Acts by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and inhibits ADP-induced platelet aggregation in human platelet-rich plasma.<ref>PMID:12450389</ref>  [[http://www.uniprot.org/uniprot/VM2AB_AGKCO VM2AB_AGKCO]] Snake venom metalloproteinase: impairs hemostasis in the envenomed animal (By similarity). This product has not been identified in the venom.  Disintegrin acostatin-beta: inhibits platelet aggregation in human platelet-rich plasma induced by ADP. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3c05 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3c05" style="background-color:#fffaf0;"></div>
 ==See Also==

3c05

From Proteopedia

Revision as of 00:03, 10 February 2016

Crystal structure of Acostatin from Agkistrodon Contortrix Contortrix

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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