1aoc: Difference between revisions

Revision as of 17:16, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1aoc.png

Template:STRUCTURE 1aoc

JAPANESE HORSESHOE CRAB COAGULOGENJAPANESE HORSESHOE CRAB COAGULOGEN

Template:ABSTRACT PUBMED 9003754

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

Page seeded by OCA on Mon Jun 30 17:16:56 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1aoc.gif|left|200px]]
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-'''JAPANESE HORSESHOE CRAB COAGULOGEN'''
+===JAPANESE HORSESHOE CRAB COAGULOGEN===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9003754}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9003754 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9003754}}
 ==About this Structure==
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 [[Category: Coagulation factor]]
 [[Category: Cystine knot superfamily]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:30:29 2008''
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