1aoc: Difference between revisions
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|PDB= 1aoc |SIZE=350|CAPTION= <scene name='initialview01'>1aoc</scene>, resolution 2.0Å | |PDB= 1aoc |SIZE=350|CAPTION= <scene name='initialview01'>1aoc</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aoc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aoc OCA], [http://www.ebi.ac.uk/pdbsum/1aoc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aoc RCSB]</span> | |||
}} | }} | ||
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[[Category: Oganessyan, V.]] | [[Category: Oganessyan, V.]] | ||
[[Category: Typke, D.]] | [[Category: Typke, D.]] | ||
[[Category: clottable protein]] | [[Category: clottable protein]] | ||
[[Category: coagulation factor]] | [[Category: coagulation factor]] | ||
[[Category: cystine knot superfamily]] | [[Category: cystine knot superfamily]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:44:20 2008'' | ||
Revision as of 18:44, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
JAPANESE HORSESHOE CRAB COAGULOGEN
OverviewOverview
The clotting cascade system of the horseshoe crab (Limulus) is involved in both haemostasis and host defence. The cascade results in the conversion of coagulogen, a soluble protein, into an insoluble coagulin gel. The clotting enzyme excises the fragment peptide C from coagulogen, giving rise to aggregation of the monomers. The crystal structure of coagulogen reveals an elongated molecule that embraces the helical peptide C fragment. Cleavage and removal of the peptide C would expose an extended hydrophobic cove, which could interact with the hydrophobic edge of a second molecule, leading to a polymeric fibre. The C-terminal half of the coagulogen molecule exhibits a striking topological similarity to the neurotrophin nerve growth factor (NGF), providing the first evidence for a neurotrophin fold in invertebrates. Similarities between coagulogen and Spatzle, the Drosophila ligand of the receptor Toll, suggest that the neurotrophin fold might be considered more ancient and widespread than previously realized.
About this StructureAbout this Structure
1AOC is a Single protein structure of sequence from Tachypleus tridentatus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor., Bergner A, Oganessyan V, Muta T, Iwanaga S, Typke D, Huber R, Bode W, EMBO J. 1996 Dec 16;15(24):6789-97. PMID:9003754
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