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3f5n

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Revision as of 22:01, 2 December 2018

Structure of native human neuroserpin

Structural highlights

3f5n is a 5 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3f02
Gene:	SERPINI1, PI12 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[NEUS_HUMAN] Familial encephalopathy with neuroserpin inclusion bodies. The disease is caused by mutations affecting the gene represented in this entry.

Function

[NEUS_HUMAN] 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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Human neuroserpin (hNS) is a protein serine protease inhibitor expressed mainly in the nervous system, where it plays key roles in neural development and plasticity by primarily targeting tissue plasminogen activator (tPA). Four hNS mutations are associated to a form of autosomal dominant dementia, known as familial encephalopathy with neuroserpin inclusion bodies. The medical interest in and the lack of structural information on hNS prompted us to study the crystal structure of native and cleaved hNS, reported here at 3.15 and 1.85 A resolution, respectively. In the light of the three-dimensional structures, we focus on the hNS reactive centre loop in its intact and cleaved conformations relative to the current serpin polymerization models and discuss the protein sites hosting neurodegenerative mutations. On the basis of homologous serpin structures, we suggest the location of a protein surface site that may stabilize the hNS native (metastable) form. In parallel, we present the results of kinetic studies on hNS inhibition of tPA. Our data analysis stresses the instability of the hNS-tPA complex with a dissociation half-life of minutes compared to a half-life of weeks observed for other serpin-cognate protease complexes.

Human neuroserpin: structure and time-dependent inhibition.,Ricagno S, Caccia S, Sorrentino G, Antonini G, Bolognesi M J Mol Biol. 2009 Apr 24;388(1):109-21. Epub 2009 Mar 2. PMID:19265707^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ricagno S, Caccia S, Sorrentino G, Antonini G, Bolognesi M. Human neuroserpin: structure and time-dependent inhibition. J Mol Biol. 2009 Apr 24;388(1):109-21. Epub 2009 Mar 2. PMID:19265707 doi:10.1016/j.jmb.2009.02.056

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3f5n"

@@ Line 1: / Line 1: @@
 ==Structure of native human neuroserpin==
 <StructureSection load='3f5n' size='340' side='right' caption='[[3f5n]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f02|3f02]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SERPINI1, PI12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3f5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f5n OCA], [http://pdbe.org/3f5n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f5n RCSB], [http://www.ebi.ac.uk/pdbsum/3f5n PDBsum]</span></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=3f5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f5n OCA], [http://pdbe.org/3f5n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f5n RCSB], [http://www.ebi.ac.uk/pdbsum/3f5n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3f5n ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f5/3f5n_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f5/3f5n_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3f5n

From Proteopedia

Revision as of 22:01, 2 December 2018

Structure of native human neuroserpin

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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