2k51: Difference between revisions
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==NMR Solution Structure of the Neurotrypsin Kringle Domain== | ==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]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k51]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2k51]] is a 1 chain structure with sequence from [https://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 [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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2k4r|2k4r]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Prss12, nt ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Prss12, nt ([https://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'>[ | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Trypsin|Trypsin]] | *[[Trypsin 3D structures|Trypsin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Buffalo rat]] | [[Category: Buffalo rat]] | ||
[[Category: Large Structures]] | |||
[[Category: Ozhogina, O A]] | [[Category: Ozhogina, O A]] | ||
[[Category: Disulfide-rich protein fold]] | [[Category: Disulfide-rich protein fold]] | ||
Revision as of 11:09, 7 April 2021
NMR Solution Structure of the Neurotrypsin Kringle DomainNMR Solution Structure of the Neurotrypsin Kringle Domain
Structural highlights
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 PubMedNeurotrypsin 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. See AlsoReferences
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