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| | <StructureSection load='1pt6' size='340' side='right'caption='[[1pt6]], [[Resolution|resolution]] 1.87Å' scene=''> | | <StructureSection load='1pt6' size='340' side='right'caption='[[1pt6]], [[Resolution|resolution]] 1.87Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pt6]] 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=1PT6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PT6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pt6]] 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=1PT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PT6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.87Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qcy|1qcy]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ITGA1 ([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=1pt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pt6 OCA], [https://pdbe.org/1pt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pt6 RCSB], [https://www.ebi.ac.uk/pdbsum/1pt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pt6 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=1pt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pt6 OCA], [http://pdbe.org/1pt6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pt6 RCSB], [http://www.ebi.ac.uk/pdbsum/1pt6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pt6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ITA1_HUMAN ITA1_HUMAN]] Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. | + | [https://www.uniprot.org/uniprot/ITA1_HUMAN ITA1_HUMAN] Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Airenne, T T]] | + | [[Category: Airenne TT]] |
| - | [[Category: Heino, J]] | + | [[Category: Heino J]] |
| - | [[Category: Johnson, M S]] | + | [[Category: Johnson MS]] |
| - | [[Category: Kapyla, J]] | + | [[Category: Kapyla J]] |
| - | [[Category: Kidron, H]] | + | [[Category: Kidron H]] |
| - | [[Category: Nyholm, T K.M]] | + | [[Category: Nyholm TKM]] |
| - | [[Category: Nymalm, Y]] | + | [[Category: Nymalm Y]] |
| - | [[Category: Pentikainen, O]] | + | [[Category: Pentikainen O]] |
| - | [[Category: Puranen, J S]] | + | [[Category: Puranen JS]] |
| - | [[Category: Salminen, T A]] | + | [[Category: Salminen TA]] |
| - | [[Category: Slotte, J P]] | + | [[Category: Slotte JP]] |
| - | [[Category: Alpha1]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Integrin]]
| + | |
| Structural highlights
Function
ITA1_HUMAN Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen.
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
Integrin alpha(1)beta(1) is one of four collagen-binding integrins in humans. Collagens bind to the alphaI domain and in the case of alpha(2)I collagen binding is competitively inhibited by peptides containing the RKKH sequence and derived from the metalloproteinase jararhagin of snake venom from Bothrops jararaca. In alpha(2)I, these peptides bind near the metal ion-dependent adhesion site (MIDAS), where a collagen (I)-like peptide is known to bind; magnesium is required for binding. Published structures of the ligand-bound "open" conformation of alpha(2)I differs significantly from the "closed" conformation seen in the structure of apo-alpha(2)I near MIDAS. Here we show that two peptides, CTRKKHDC and CARKKHDC, derived from jararhagin also bind to alpha(1)I and competitively inhibit collagen I binding. Furthermore, calorimetric and fluorimetric measurements show that the structure of the complex of alpha(1)I with Mg(2+) and CTRKKHDC differs from structure in the absence of peptide. A comparison of the x-ray structure of apo-alpha(1)I ("closed" conformation) and a model structure of the alpha(1)I ("open" conformation) based on the closely related structure of alpha(2)I reveals that the binding site is partially blocked to ligands by Glu(255) and Tyr(285) in the "closed" structure, whereas in the "open" structure helix C is unwound and these residues are shifted, and the "RKKH" peptides fit well when docked. The "open" conformation of alpha(2)I resulting from binding a collagen (I)-like peptide leads to exposure of hydrophobic surface, also seen in the model of alpha(1)I and shown experimentally for alpha(1)I using a fluorescent hydrophobic probe.
Jararhagin-derived RKKH peptides induce structural changes in alpha1I domain of human integrin alpha1beta1.,Nymalm Y, Puranen JS, Nyholm TK, Kapyla J, Kidron H, Pentikainen OT, Airenne TT, Heino J, Slotte JP, Johnson MS, Salminen TA J Biol Chem. 2004 Feb 27;279(9):7962-70. Epub 2003 Dec 4. PMID:14660600[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nymalm Y, Puranen JS, Nyholm TK, Kapyla J, Kidron H, Pentikainen OT, Airenne TT, Heino J, Slotte JP, Johnson MS, Salminen TA. Jararhagin-derived RKKH peptides induce structural changes in alpha1I domain of human integrin alpha1beta1. J Biol Chem. 2004 Feb 27;279(9):7962-70. Epub 2003 Dec 4. PMID:14660600 doi:http://dx.doi.org/10.1074/jbc.M312912200
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