1iod

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CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE COAGULATION FACTOR X BINDING PROTEIN FROM SNAKE VENOM AND THE GLA DOMAIN OF FACTOR XCRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE COAGULATION FACTOR X BINDING PROTEIN FROM SNAKE VENOM AND THE GLA DOMAIN OF FACTOR X

Structural highlights

1iod is a 3 chain structure with sequence from Bos taurus and Deinagkistrodon acutus. The March 2006 RCSB PDB Molecule of the Month feature on Tissue Factor by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SLUA_DEIAC Anticoagulant protein which binds to the gamma-carboxyglutamic acid-domain regions of factors IX (F9) and factor X (F10) in the presence of calcium with a 1 to 1 stoichiometry. Also inhibits platelet aggregation by binding to platelet glycoprotein Ibalpha (GP1BA) and functioning as a blocker of von Willebrand factor (VWF). Is devoid of hemorrhagic and lethal activities. Possesses antithrombotic and thrombolytic activities. Also hydrolyzes the Aalpha-chain of fibrinogen (FGA). Does not affect the Bbeta-chain (FGB) and the gamma chain (FGG).[1] [2] [3]

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 gamma-carboxyglutamic acid (Gla) domain of blood coagulation factors is responsible for Ca2+-dependent phospholipid membrane binding. Factor X-binding protein (X-bp), an anticoagulant protein from snake venom, specifically binds to the Gla domain of factor X. The crystal structure of X-bp in complex with the Gla domain peptide of factor X at 2.3-A resolution showed that the anticoagulation is based on the fact that two patches of the Gla domain essential for membrane binding are buried in the complex formation. The Gla domain thus is expected to be a new target of anticoagulant drugs, and X-bp provides a basis for designing them. This structure also provides a membrane-bound model of factor X.

Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X.,Mizuno H, Fujimoto Z, Atoda H, Morita T Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7230-4. Epub 2001 Jun 12. PMID:11404471[4]

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

See Also

References

  1. ↑ Cheng X, Qian Y, Liu Q, Li BX, Zhang M, Liu J. Purification, characterization, and cDNA cloning of a new fibrinogenlytic venom protein, Agkisacutacin, from Agkistrodon acutus venom. Biochem Biophys Res Commun. 1999 Nov 19;265(2):530-5. PMID:10558903 doi:10.1006/bbrc.1999.1685
  2. ↑ Cheng X, Xu ZY, Liu QD, Li XM, Li XY, Liu J. Purification and Characterization of a Platelet Agglutinating Inhibiting Protein (Agkisacutacin) from Agkistrodon acutus Venom. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2000;32(6):653-656 PMID:12058182
  3. ↑ Li WF, Chen L, Li XM, Liu J. A C-type lectin-like protein from Agkistrodon acutus venom binds to both platelet glycoprotein Ib and coagulation factor IX/factor X. Biochem Biophys Res Commun. 2005 Jul 8;332(3):904-12. PMID:15925567 doi:10.1016/j.bbrc.2005.05.033
  4. ↑ Mizuno H, Fujimoto Z, Atoda H, Morita T. Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X. Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7230-4. Epub 2001 Jun 12. PMID:11404471 doi:10.1073/pnas.131179698

1iod, resolution 2.30Å

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