1i8n

CRYSTAL STRUCTURE OF LEECH ANTI-PLATELET PROTEIN

spinqualitylabelsall models 1i8n, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1i8n is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ROP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LAPP_HAEOF] An inhibitor of collagen-stimulated platelet aggregation, dense granule release and serotonin release. Publication Abstract from PubMed Leech anti-platelet protein (LAPP) from the leech Haementeria officinalis is a collagen-binding protein that inhibits the collagen-mediated adhesion of blood platelets. The crystal structure of recombinant LAPP has been determined using single isomorphous replacement with anomalous scattering combined with solvent flattening and threefold molecular averaging. The model of LAPP has been refined to 2.2 A resolution (R factor 21.5%; free R factor 24.0%). LAPP contains an 89-residue C-terminal domain consisting of a central six-stranded antiparallel beta-sheet flanked on one side by an alpha-helix and on the other side by two extended loops with little secondary structure. A 36-residue N-terminal region is not visible in the electron-density map. This region is rich in glycine and lacks hydrophobic residues. It probably does not have a compact globular fold, but instead has an extended conformation and is flexible. The crystal packing suggests that LAPP may form tightly interacting dimers. The fold of the C-terminal domain of LAPP closely resembles that of the N-domain of hepatocyte growth factor (HGF), which classifies LAPP as a PAN domain. However, no significant sequence homology exists between LAPP and other PAN domains. Common structural features between LAPP and the HGF N-domain include two disulfide bonds that link the alpha-helix to the central region of the protein and five residues with a conserved hydrophobic nature that are located in the core of the domain. These conserved structural features may be an important determinant of the PAN-domain type of fold. The structure of leech anti-platelet protein, an inhibitor of haemostasis.,Huizinga EG, Schouten A, Connolly TM, Kroon J, Sixma JJ, Gros P Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1071-8. Epub 2001, Jul 23. PMID:11468390 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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