1npm

From Proteopedia

(Difference between revisions)

Revision as of 09:47, 1 November 2017

NEUROPSIN, A SERINE PROTEASE EXPRESSED IN THE LIMBIC SYSTEM OF MOUSE BRAIN

Structural highlights

1npm is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KLK8_MOUSE] Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. Involved in skin desquamation and keratinocyte proliferation. Plays a role in the secondary phase of pathogenesis following spinal cord injury.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

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

Neuropsin is a novel serine protease, the expression of which is highly localized in the limbic areas of the mouse brain and which is suggested to be involved in kindling epileptogenesis and hippocampal plasticity. The 2.1-A resolution crystal structure of neuropsin provides the first three-dimensional view of one of the serine proteases highly expressed in the nervous system, and reveals a serine protease fold that exhibits chimeric features between trypsin and nerve growth factor-gamma (NGFgamma), a member of the kallikrein family. Neuropsin possesses an N-glycosylated "kallikrein loop" but forms six disulfide bonds corresponding to those of trypsin. The ordered kallikrein loop projects proline toward the active site to restrict smaller residues or proline at the P2 position of substrates. Loop F, which participates in forming the S3/S4 sites, is similar to trypsin rather than NGFgamma. The unique conformations of loops G and H form an S1 pocket specific for both arginine and lysine. These characteristic loop structures forming the substrate-binding site suggest the novel substrate specificity of neuropsin and give a clue to the design of its specific inhibitors.

Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis.,Kishi T, Kato M, Shimizu T, Kato K, Matsumoto K, Yoshida S, Shiosaka S, Hakoshima T J Biol Chem. 1999 Feb 12;274(7):4220-4. PMID:9933620^[9]

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

References

↑ Shimizu C, Yoshida S, Shibata M, Kato K, Momota Y, Matsumoto K, Shiosaka T, Midorikawa R, Kamachi T, Kawabe A, Shiosaka S. Characterization of recombinant and brain neuropsin, a plasticity-related serine protease. J Biol Chem. 1998 May 1;273(18):11189-96. PMID:9556608
↑ Komai S, Matsuyama T, Matsumoto K, Kato K, Kobayashi M, Imamura K, Yoshida S, Ugawa S, Shiosaka S. Neuropsin regulates an early phase of schaffer-collateral long-term potentiation in the murine hippocampus. Eur J Neurosci. 2000 Apr;12(4):1479-86. PMID:10762375
↑ Oka T, Akisada M, Okabe A, Sakurai K, Shiosaka S, Kato K. Extracellular serine protease neuropsin (KLK8) modulates neurite outgrowth and fasciculation of mouse hippocampal neurons in culture. Neurosci Lett. 2002 Mar 22;321(3):141-4. PMID:11880192
↑ Matsumoto-Miyai K, Ninomiya A, Yamasaki H, Tamura H, Nakamura Y, Shiosaka S. NMDA-dependent proteolysis of presynaptic adhesion molecule L1 in the hippocampus by neuropsin. J Neurosci. 2003 Aug 27;23(21):7727-36. PMID:12944500
↑ Nakamura Y, Tamura H, Horinouchi K, Shiosaka S. Role of neuropsin in formation and maturation of Schaffer-collateral L1cam-immunoreactive synaptic boutons. J Cell Sci. 2006 Apr 1;119(Pt 7):1341-9. Epub 2006 Mar 14. PMID:16537644 doi:http://dx.doi.org/10.1242/jcs.02862
↑ Tamura H, Ishikawa Y, Hino N, Maeda M, Yoshida S, Kaku S, Shiosaka S. Neuropsin is essential for early processes of memory acquisition and Schaffer collateral long-term potentiation in adult mouse hippocampus in vivo. J Physiol. 2006 Feb 1;570(Pt 3):541-51. Epub 2005 Nov 24. PMID:16308352 doi:http://dx.doi.org/jphysiol.2005.098715
↑ Kishibe M, Bando Y, Terayama R, Namikawa K, Takahashi H, Hashimoto Y, Ishida-Yamamoto A, Jiang YP, Mitrovic B, Perez D, Iizuka H, Yoshida S. Kallikrein 8 is involved in skin desquamation in cooperation with other kallikreins. J Biol Chem. 2007 Feb 23;282(8):5834-41. Epub 2006 Dec 19. PMID:17182622 doi:http://dx.doi.org/M607998200
↑ Terayama R, Bando Y, Murakami K, Kato K, Kishibe M, Yoshida S. Neuropsin promotes oligodendrocyte death, demyelination and axonal degeneration after spinal cord injury. Neuroscience. 2007 Aug 10;148(1):175-87. Epub 2007 Jul 12. PMID:17629414 doi:http://dx.doi.org/10.1016/j.neuroscience.2007.05.037
↑ Kishi T, Kato M, Shimizu T, Kato K, Matsumoto K, Yoshida S, Shiosaka S, Hakoshima T. Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis. J Biol Chem. 1999 Feb 12;274(7):4220-4. PMID:9933620

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1npm"

@@ Line 1: / Line 1: @@
 ==NEUROPSIN, A SERINE PROTEASE EXPRESSED IN THE LIMBIC SYSTEM OF MOUSE BRAIN==
 <StructureSection load='1npm' size='340' side='right' caption='[[1npm]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1npm]] is a 2 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=1NPM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NPM FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1npm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1npm OCA], [http://pdbe.org/1npm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1npm RCSB], [http://www.ebi.ac.uk/pdbsum/1npm 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=1npm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1npm OCA], [http://pdbe.org/1npm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1npm RCSB], [http://www.ebi.ac.uk/pdbsum/1npm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1npm ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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].
+</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/main_output.php?pdb_ID=1npm ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1npm

From Proteopedia

Revision as of 09:47, 1 November 2017

NEUROPSIN, A SERINE PROTEASE EXPRESSED IN THE LIMBIC SYSTEM OF MOUSE BRAIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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