2k51

From Proteopedia

(Difference between revisions)

Current revision

NMR Solution Structure of the Neurotrypsin Kringle Domain

Structural highlights

2k51 is a 1 chain structure with sequence from Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 1 model
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NETR_RAT Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.

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

Neurotrypsin is a multidomain protein that serves as a brain-specific serine protease. Here we report the NMR structure of its kringle domain, NT/K. The data analysis was performed with the BACUS (Bayesian analysis of coupled unassigned spins) algorithm. This study presents the first application of BACUS to the structure determination of a (13)C unenriched protein for which no prior experimental 3D structure was available. NT/K adopts the kringle fold, consisting of an antiparallel beta-sheet bridged by an overlapping pair of disulfides. The structure reveals the presence of a surface-exposed left-handed polyproline II helix that is closely packed to the core beta-structure. This feature distinguishes NT/K from other members of the kringle fold and points toward a novel functional role for a kringle domain. Functional divergence among kringle domains is discussed on the basis of their surface and electrostatic characteristics.

NMR Solution Structure of the Neurotrypsin Kringle Domain.,Ozhogina OA, Grishaev A, Bominaar EL, Patthy L, Trexler M, Llinas M Biochemistry. 2008 Oct 29. PMID:18956887^[1]

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

References

↑ Ozhogina OA, Grishaev A, Bominaar EL, Patthy L, Trexler M, Llinas M. NMR Solution Structure of the Neurotrypsin Kringle Domain. Biochemistry. 2008 Oct 29. PMID:18956887 doi:10.1021/bi800555z

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k51"

Categories: Large Structures | Rattus norvegicus | Ozhogina OA

@@ Line 1: / Line 1: @@
 ==NMR Solution Structure of the Neurotrypsin Kringle Domain==
-<StructureSection load='2k51' size='340' side='right' caption='[[2k51]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='2k51' size='340' side='right'caption='[[2k51]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2k51]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K51 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K51 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2k51]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K51 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k4r|2k4r]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Prss12, nt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=2k51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k51 OCA], [https://pdbe.org/2k51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k51 RCSB], [https://www.ebi.ac.uk/pdbsum/2k51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k51 ProSAT]</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=2k51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k51 OCA], [http://pdbe.org/2k51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k51 RCSB], [http://www.ebi.ac.uk/pdbsum/2k51 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k51 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/NETR_RAT NETR_RAT]] Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.
+[https://www.uniprot.org/uniprot/NETR_RAT NETR_RAT] Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 15: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k5/2k51_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 31: / Line 30: @@
 ==See Also==
-*[[Trypsin|Trypsin]]
+*[[Trypsin 3D structures|Trypsin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
+[[Category: Large Structures]]
-[[Category: Ozhogina, O A]]
+[[Category: Rattus norvegicus]]
-[[Category: Disulfide-rich protein fold]]
+[[Category: Ozhogina OA]]
-[[Category: Extracellular proteolysis]]
-[[Category: Hydrolase]]
-[[Category: Kringle domain]]
-[[Category: Neurotrypsin]]
-[[Category: Serine endopeptidase]]

2k51

From Proteopedia

Current revision

NMR Solution Structure of the Neurotrypsin Kringle Domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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