1jjo

<StructureSection load='1jjo' size='340' side='right' caption='[[1jjo]], [[Resolution|resolution]] 3.06&Aring;' scene=''>

<table><tr><td colspan='2'>[[1jjo]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JJO FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SERPINI1 or PI12 or SPI17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jjo OCA], [http://pdbe.org/1jjo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jjo RCSB], [http://www.ebi.ac.uk/pdbsum/1jjo PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/NEUS_MOUSE NEUS_MOUSE]] Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jj/1jjo_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

The protease inhibitor neuroserpin regulates the development of the nervous system and its plasticity in the adult. Neuroserpins carrying the Ser53Pro or Ser56Arg mutation form polymers in neuronal cells. We describe here the structure of wild-type neuroserpin in a cleaved form. The structure provides a basis to understand the role of the mutations in the polymerization process. We propose that these mutations could delay the insertion of the reactive center loop into the central beta-sheet A, an essential step in the inhibition and possibly in the polymerization of neuroserpin.

Crystal structure of neuroserpin: a neuronal serpin involved in a conformational disease.,Briand C, Kozlov SV, Sonderegger P, Grutter MG FEBS Lett. 2001 Sep 7;505(1):18-22. PMID:11557034<ref>PMID:11557034</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1jjo" style="background-color:#fffaf0;"></div>

*[[Serpin|Serpin]]

[[Category: Lk3 transgenic mice]]

[[Category: Briand, C]]

[[Category: Gruetter, M G]]

[[Category: Kozlov, S V]]

[[Category: Sonderegger, P]]

[[Category: Neuronal serpin]]

[[Category: Signaling protein]]