1aoc: Difference between revisions
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[[Image:1aoc.gif|left|200px]] | [[Image:1aoc.gif|left|200px]] | ||
'''JAPANESE HORSESHOE CRAB COAGULOGEN''' | {{Structure | ||
|PDB= 1aoc |SIZE=350|CAPTION= <scene name='initialview01'>1aoc</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''JAPANESE HORSESHOE CRAB COAGULOGEN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AOC is a [ | 1AOC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOC OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9003754 9003754] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tachypleus tridentatus]] | [[Category: Tachypleus tridentatus]] | ||
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[[Category: cystine knot superfamily]] | [[Category: cystine knot superfamily]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:12 2008'' | ||
Revision as of 11:00, 20 March 2008
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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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