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| ==Tim-1== | | ==Tim-1== |
- | <StructureSection load='2or8' size='340' side='right' caption='[[2or8]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='2or8' size='340' side='right'caption='[[2or8]], [[Resolution|resolution]] 2.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2or8]] 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=2OR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OR8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2or8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OR8 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2or7|2or7]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Havcr1, Tim1, Timd1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=2or8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2or8 OCA], [https://pdbe.org/2or8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2or8 RCSB], [https://www.ebi.ac.uk/pdbsum/2or8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2or8 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=2or8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2or8 OCA], [http://pdbe.org/2or8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2or8 RCSB], [http://www.ebi.ac.uk/pdbsum/2or8 PDBsum]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/HAVR1_MOUSE HAVR1_MOUSE]] May play a role in T-helper cell development and the regulation of asthma and allergic diseases. Receptor for TIMD4. May play a role in kidney injury and repair (By similarity). | + | [https://www.uniprot.org/uniprot/HAVR1_MOUSE HAVR1_MOUSE] May play a role in T-helper cell development and the regulation of asthma and allergic diseases. Receptor for TIMD4. May play a role in kidney injury and repair (By similarity). |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Check<jmol> | | Check<jmol> |
| <jmolCheckbox> | | <jmolCheckbox> |
- | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/or/2or8_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/or/2or8_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> | | <text>to colour the structure by Evolutionary Conservation</text> |
| </jmolCheckbox> | | </jmolCheckbox> |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
- | [[Category: Ballesteros, A]] | + | [[Category: Mus musculus]] |
- | [[Category: Casasnovas, J M]] | + | [[Category: Ballesteros A]] |
- | [[Category: Kaplan, G G]] | + | [[Category: Casasnovas JM]] |
- | [[Category: Santiago, C]] | + | [[Category: Kaplan GG]] |
- | [[Category: Beta barrel]] | + | [[Category: Santiago C]] |
- | [[Category: Igv domain]]
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- | [[Category: Immune system]]
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- | [[Category: Immunoglobulin fold]]
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- | [[Category: Tim]]
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| Structural highlights
Function
HAVR1_MOUSE May play a role in T-helper cell development and the regulation of asthma and allergic diseases. Receptor for TIMD4. May play a role in kidney injury and repair (By similarity).
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
The T cell immunoglobulin mucin (TIM) receptors are involved in the regulation of immune responses, autoimmunity, and allergy. Structures of the N-terminal ligand binding domain of the murine mTIM-1 and mTIM-2 receptors revealed an immunoglobulin (Ig) fold, with four Cys residues bridging a distinctive CC' loop to the GFC beta-sheet. The structures showed two ligand-recognition modes in the TIM family. The mTIM-1 structure identified a homophilic TIM-TIM adhesion interaction, whereas the mTIM-2 domain formed a dimer that prevented homophilic binding. Biochemical, mutational, and cell adhesion analyses confirmed the divergent ligand-binding modes revealed by the structures. Structural features characteristic of mTIM-1 appear conserved in human TIM-1, which also mediated homophilic interactions. The extracellular mucin domain enhanced binding through the Ig domain, modulating TIM receptor functions. These results explain the divergent immune functions described for the murine receptors and the role of TIM-1 as a cell adhesion receptor in renal regeneration and cancer.
Structures of T Cell immunoglobulin mucin receptors 1 and 2 reveal mechanisms for regulation of immune responses by the TIM receptor family.,Santiago C, Ballesteros A, Tami C, Martinez-Munoz L, Kaplan GG, Casasnovas JM Immunity. 2007 Mar;26(3):299-310. PMID:17363299[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Santiago C, Ballesteros A, Tami C, Martinez-Munoz L, Kaplan GG, Casasnovas JM. Structures of T Cell immunoglobulin mucin receptors 1 and 2 reveal mechanisms for regulation of immune responses by the TIM receptor family. Immunity. 2007 Mar;26(3):299-310. PMID:17363299 doi:http://dx.doi.org/10.1016/j.immuni.2007.01.014
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