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| | <StructureSection load='4neh' size='340' side='right'caption='[[4neh]], [[Resolution|resolution]] 2.75Å' scene=''> | | <StructureSection load='4neh' size='340' side='right'caption='[[4neh]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4neh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NEH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4NEH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4neh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NEH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.7505Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k6s|3k6s]], [[3k71|3k71]], [[3k7s|3k7s]], [[2iue|2iue]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ITGAX, CD11C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ITGB2, CD18, MFI7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4neh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4neh OCA], [https://pdbe.org/4neh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4neh RCSB], [https://www.ebi.ac.uk/pdbsum/4neh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4neh ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4neh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4neh OCA], [http://pdbe.org/4neh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4neh RCSB], [http://www.ebi.ac.uk/pdbsum/4neh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4neh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | == Disease == | |
| - | [[http://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN]] Defects in ITGB2 are the cause of leukocyte adhesion deficiency type 1 (LAD1) [MIM:[http://omim.org/entry/116920 116920]]. LAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions.<ref>PMID:7509236</ref> <ref>PMID:1346613</ref> <ref>PMID:1968911</ref> <ref>PMID:1694220</ref> <ref>PMID:1590804</ref> <ref>PMID:1352501</ref> <ref>PMID:1347532</ref> <ref>PMID:7686755</ref> <ref>PMID:9884339</ref> <ref>PMID:20529581</ref> <ref>PMID:20549317</ref> | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ITAX_HUMAN ITAX_HUMAN]] Integrin alpha-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis. [[http://www.uniprot.org/uniprot/ITB2_HUMAN ITB2_HUMAN]] Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin alpha-X/beta-2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation.<ref>PMID:18587400</ref> | + | [https://www.uniprot.org/uniprot/ITAX_HUMAN ITAX_HUMAN] Integrin alpha-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sen, M]] | + | [[Category: Sen M]] |
| - | [[Category: Springer, T A]] | + | [[Category: Springer TA]] |
| - | [[Category: Yuki, K]] | + | [[Category: Yuki K]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Complement receptor]]
| + | |
| - | [[Category: Denaturated protein]]
| + | |
| - | [[Category: Fibrinogen]]
| + | |
| - | [[Category: Heparin]]
| + | |
| - | [[Category: Ic3b]]
| + | |
| - | [[Category: Icam-1]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: N-linked glycosylation]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
4neh is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.7505Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
ITAX_HUMAN Integrin alpha-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis.
Publication Abstract from PubMed
How is massive conformational change in integrins achieved on a rapid timescale? We report crystal structures of a metastable, putative transition state of integrin alphaXbeta2. The alphaXbeta2 ectodomain is bent; however, a lattice contact stabilizes its ligand-binding alphaI domain in a high affinity, open conformation. Much of the alphaI alpha7 helix unwinds, loses contact with the alphaI domain, and reshapes to form an internal ligand that binds to the interface between the beta propeller and betaI domains. Lift-off of the alphaI domain above this platform enables a range of extensional and rotational motions without precedent in allosteric machines. Movements of secondary structure elements in the beta2 betaI domain occur in an order different than in beta3 integrins, showing that integrin beta subunits can be specialized to assume different intermediate states between closed and open. Mutations demonstrate that the structure trapped here is metastable and can enable rapid equilibration between bent and extended-open integrin conformations and up-regulation of leukocyte adhesiveness.
An internal ligand-bound, metastable state of a leukocyte integrin, alphaXbeta2.,Sen M, Yuki K, Springer TA J Cell Biol. 2013 Nov 25;203(4):629-42. doi: 10.1083/jcb.201308083. PMID:24385486[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sen M, Yuki K, Springer TA. An internal ligand-bound, metastable state of a leukocyte integrin, alphaXbeta2. J Cell Biol. 2013 Nov 25;203(4):629-42. doi: 10.1083/jcb.201308083. PMID:24385486 doi:http://dx.doi.org/10.1083/jcb.201308083
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