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| | ==Pactolus I-domain: Functional Switching of the Rossmann Fold== | | ==Pactolus I-domain: Functional Switching of the Rossmann Fold== |
| - | <StructureSection load='2iue' size='340' side='right'caption='[[2iue]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2iue' size='340' side='right'caption='[[2iue]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2iue]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IUE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2iue]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IUE FirstGlance]. <br> |
| - | </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=2iue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iue OCA], [https://pdbe.org/2iue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iue RCSB], [https://www.ebi.ac.uk/pdbsum/2iue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iue ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2iue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iue OCA], [https://pdbe.org/2iue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iue RCSB], [https://www.ebi.ac.uk/pdbsum/2iue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iue ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ITB2L_MOUSE ITB2L_MOUSE]] During inflammatory stimulation, plays a role in retaining Cxcl13-expressing cells at the site of the inflammatory response.<ref>PMID:16836649</ref>
| + | [https://www.uniprot.org/uniprot/ITB2L_MOUSE ITB2L_MOUSE] During inflammatory stimulation, plays a role in retaining Cxcl13-expressing cells at the site of the inflammatory response.<ref>PMID:16836649</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Legge, G B]] | + | [[Category: Legge GB]] |
| - | [[Category: Sen, M]] | + | [[Category: Sen M]] |
| - | [[Category: Admida]]
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| - | [[Category: Cd]]
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| - | [[Category: Cell adhesion]]
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| - | [[Category: Integrin]]
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| - | [[Category: Itc]]
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| - | [[Category: Limb]]
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| - | [[Category: Membrane]]
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| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Mida]]
| + | |
| - | [[Category: Titration]]
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| - | [[Category: Transmembrane]]
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| Structural highlights
Function
ITB2L_MOUSE During inflammatory stimulation, plays a role in retaining Cxcl13-expressing cells at the site of the inflammatory response.[1]
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
Murine Pactolus is a neutrophil-specific single chain glycoprotein that plays a role as an apoptosis marker for macrophages. The extracellular region of the protein shows strong sequence similarities to integrin beta-subunits. Critical sequence modifications differentiate its function when compared to the integrin family. We show experimentally that Pactolus I-domain does not bind divalent metal ions, indicating that ligand binding is not mediated through a metal ion-dependent adhesion site (MIDAS). NMR data was used to map secondary structure and the strand pairing within the beta-sheet to confirm an overall Rossmann fold topology. Homology modeling enhanced by the NMR data was used to determine the overall structure, with two key loop insertions/deletions (insertion 2 and SDL) that distinguish the Pactolus I-domain from the integrin alpha I-domain and beta I-domains. NMR peak exchange broadening is observed due to dimerization, correlating to the beta I-domain and beta propeller heterodimerization region within the integrin headpiece. Two unique N-linked glycosylation sites (Asn151 and Asn230) within this region disrupt dimerization and may account for why Pactolus is not found to associate with an alpha-subunit. These changes in quaternary structure, ligand binding loops, glycosylation, and metal sites illustrate how evolution has rapidly and effectively altered key aspects of the integrin beta-subunit to derive a protein of novel function on an existing protein scaffold.
Pactolus I-domain: functional switching of the Rossmann fold.,Sen M, Legge GB Proteins. 2007 Aug 15;68(3):626-35. PMID:17523188[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hojgaard A, Close R, Dunn DM, Weiss RB, Weis JJ, Weis JH. Altered localization of CXCL13 expressing cells in mice deficient in Pactolus following an inflammatory stimulus. Immunology. 2006 Oct;119(2):212-23. Epub 2006 Jul 12. PMID:16836649 doi:http://dx.doi.org/IMM2426
- ↑ Sen M, Legge GB. Pactolus I-domain: functional switching of the Rossmann fold. Proteins. 2007 Aug 15;68(3):626-35. PMID:17523188 doi:10.1002/prot.21458
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