3bdb: Difference between revisions

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New page: '''Unreleased structure''' The entry 3bdb is ON HOLD Authors: Ostrov, D.A., Hernandez-Prada, J.A., Haire, R.N., Cannon, J.P., Magis, A.T., Bailey, K.., Litman, G.W. Description: Crysta...
 
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'''Unreleased structure'''


The entry 3bdb is ON HOLD
==Crystal Structure of Novel Immune-Type Receptor 11 Extracellular Fragment from Ictalurus punctatus including Stalk Region==
<StructureSection load='3bdb' size='340' side='right'caption='[[3bdb]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3bdb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Ictalurus_punctatus Ictalurus punctatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BDB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=3bdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bdb OCA], [https://pdbe.org/3bdb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bdb RCSB], [https://www.ebi.ac.uk/pdbsum/3bdb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bdb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8UWK4_ICTPU Q8UWK4_ICTPU]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bd/3bdb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <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/main_output.php?pdb_ID=3bdb ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Novel immune-type receptors (NITRs) comprise an exceptionally large, diversified family of activating and inhibitory receptors that has been identified in bony fish. Here, we characterized the structure of an activating NITR that is expressed by a cytotoxic natural killer (NK)-like cell line and that specifically binds an allogeneic B cell target. A single amino acid residue within the NITR immunoglobulin variable (V)-type domain accounts for specificity of the interaction. Structures solved by X-ray crystallography revealed that the V-type domains of NITRs form homodimers resembling rearranging antigen-binding receptor heterodimers. CDR1 elements of both subunits of NITR dimers form ligand-binding surfaces that determine specificity for the nonself target. In the evolution of immune function, it appears that a specific NK type of innate recognition may be mediated by a complex germline multigene family of V structures resembling those that are somatically diversified in adaptive immunological responses.


Authors: Ostrov, D.A., Hernandez-Prada, J.A., Haire, R.N., Cannon, J.P., Magis, A.T., Bailey, K.., Litman, G.W.
A bony fish immunological receptor of the NITR multigene family mediates allogeneic recognition.,Cannon JP, Haire RN, Magis AT, Eason DD, Winfrey KN, Hernandez Prada JA, Bailey KM, Jakoncic J, Litman GW, Ostrov DA Immunity. 2008 Aug 15;29(2):228-37. Epub 2008 Jul 31. PMID:18674935<ref>PMID:18674935</ref>


Description: Crystal Structure of Novel Immune-Type Receptor 11 Extracellular Fragment from Ictalurus punctatus including Stalk Region
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
 
<div class="pdbe-citations 3bdb" style="background-color:#fffaf0;"></div>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 09:25:19 2008''
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ictalurus punctatus]]
[[Category: Large Structures]]
[[Category: Bailey KM]]
[[Category: Cannon JP]]
[[Category: Haire RN]]
[[Category: Hernandez Prada JA]]
[[Category: Litman GW]]
[[Category: Magis AT]]
[[Category: Ostrov DA]]

Latest revision as of 15:07, 30 August 2023

Crystal Structure of Novel Immune-Type Receptor 11 Extracellular Fragment from Ictalurus punctatus including Stalk RegionCrystal Structure of Novel Immune-Type Receptor 11 Extracellular Fragment from Ictalurus punctatus including Stalk Region

Structural highlights

3bdb is a 6 chain structure with sequence from Ictalurus punctatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8UWK4_ICTPU

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

Novel immune-type receptors (NITRs) comprise an exceptionally large, diversified family of activating and inhibitory receptors that has been identified in bony fish. Here, we characterized the structure of an activating NITR that is expressed by a cytotoxic natural killer (NK)-like cell line and that specifically binds an allogeneic B cell target. A single amino acid residue within the NITR immunoglobulin variable (V)-type domain accounts for specificity of the interaction. Structures solved by X-ray crystallography revealed that the V-type domains of NITRs form homodimers resembling rearranging antigen-binding receptor heterodimers. CDR1 elements of both subunits of NITR dimers form ligand-binding surfaces that determine specificity for the nonself target. In the evolution of immune function, it appears that a specific NK type of innate recognition may be mediated by a complex germline multigene family of V structures resembling those that are somatically diversified in adaptive immunological responses.

A bony fish immunological receptor of the NITR multigene family mediates allogeneic recognition.,Cannon JP, Haire RN, Magis AT, Eason DD, Winfrey KN, Hernandez Prada JA, Bailey KM, Jakoncic J, Litman GW, Ostrov DA Immunity. 2008 Aug 15;29(2):228-37. Epub 2008 Jul 31. PMID:18674935[1]

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

References

  1. Cannon JP, Haire RN, Magis AT, Eason DD, Winfrey KN, Hernandez Prada JA, Bailey KM, Jakoncic J, Litman GW, Ostrov DA. A bony fish immunological receptor of the NITR multigene family mediates allogeneic recognition. Immunity. 2008 Aug 15;29(2):228-37. Epub 2008 Jul 31. PMID:18674935 doi:10.1016/j.immuni.2008.05.018

3bdb, resolution 2.80Å

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