View source for 1aoc


==JAPANESE HORSESHOE CRAB COAGULOGEN==
<StructureSection load='1aoc' size='340' side='right'caption='[[1aoc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1aoc]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aoc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aoc OCA], [https://pdbe.org/1aoc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aoc RCSB], [https://www.ebi.ac.uk/pdbsum/1aoc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aoc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COAG_TACTR COAG_TACTR] Coagulogen is a gel-forming protein of hemolymph; it hinders the spread of invaders by immobilizing them.
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== Publication Abstract from PubMed ==
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.

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<ref>PMID:9003754</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1aoc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tachypleus tridentatus]]
[[Category: Bergner A]]
[[Category: Bode W]]
[[Category: Huber R]]
[[Category: Iwanaga S]]
[[Category: Muta T]]
[[Category: Oganessyan V]]
[[Category: Typke D]]