PDBsum entry 1l3x

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protein links
Protein binding PDB id
Jmol PyMol
Protein chain
73 a.a. *
* Residue conservation analysis
PDB id:
Name: Protein binding
Title: Solution structure of novel disintegrin salmosin
Structure: Platelet aggregation inhibitor disintegrin. Chain: a. Fragment: residues 1-73. Synonym: salmosin
Source: Gloydius blomhoffi brevicaudus. Organism_taxid: 259325. Strain: brevicaudus
NMR struc: 20 models
Authors: J.Shin,W.Lee
Key ref:
J.Shin et al. (2003). Solution structure of a novel disintegrin, salmosin, from Agkistrondon halys venom. Biochemistry, 42, 14408-14415. PubMed id: 14661951 DOI: 10.1021/bi0300276
01-Mar-02     Release date:   23-Dec-03    
Supersedes: 1iq2
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q90WC0  (VM2HS_GLOBR) -  Zinc metalloproteinase/disintegrin (Fragment)
317 a.a.
73 a.a.
Key:    PfamA domain  Secondary structure  CATH domain


DOI no: 10.1021/bi0300276 Biochemistry 42:14408-14415 (2003)
PubMed id: 14661951  
Solution structure of a novel disintegrin, salmosin, from Agkistrondon halys venom.
J.Shin, S.Y.Hong, K.Chung, I.Kang, Y.Jang, D.S.Kim, W.Lee.
Disintegrins are potent inhibitors of both platelet aggregation and integrin-dependent cell adhesion. A new disintegrin, salmosin, isolated from the venom of the Korean snake Agkistrodon halys brevicaudus, has been characterized by mass spectrometry and NMR spectroscopy, and its in vitro biological activity has been assessed. The IC(50) value of the purified salmosin was determined to be 2.2 nM in an assay for the inhibition of glycoprotein IIb-IIIa/fibrinogen interaction. Salmosin also inhibited the bovine capillary endothelial cell proliferation induced by bFGF in a dose-dependent manner. The NMR solution structures were well converged with a root-mean-square deviation of 0.76 A for backbone atoms among the 20 lowest energy structures, except for the arginylglycylaspartic acid (RGD) loop. The structure revealed that the conserved RGD motif with an unusual finger shape is distal from the rigid core of the C-terminal domain. Furthermore, even though the RGD motif did not interact with the hydrophobic core of the protein, it was stabilized by a network of molecular contacts through a small antiparallel beta-sheet comprising residues of Ile46-Ala50 and Asp54-Tyr58. Last, the electrostatic charge distribution on the surface of salmosin differs dramatically from that of other disintegrin proteins in that there is a cluster of negatively charged residues in close proximity to the RGD loop.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18391413 N.Moiseeva, R.Bau, S.D.Swenson, F.S.Markland, J.Y.Choe, Z.J.Liu, and M.Allaire (2008).
Structure of acostatin, a dimeric disintegrin from Southern copperhead (Agkistrodon contortrix contortrix), at 1.7 A resolution.
  Acta Crystallogr D Biol Crystallogr, 64, 466-470.
PDB code: 3c05
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