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5hgj

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<StructureSection load='5hgj' size='340' side='right'caption='[[5hgj]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='5hgj' size='340' side='right'caption='[[5hgj]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5hgj]] 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=5HGJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HGJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5hgj]] 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=5HGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HGJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.399&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<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=5hgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hgj OCA], [http://pdbe.org/5hgj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hgj RCSB], [http://www.ebi.ac.uk/pdbsum/5hgj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hgj ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hgj OCA], [https://pdbe.org/5hgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hgj RCSB], [https://www.ebi.ac.uk/pdbsum/5hgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hgj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Integrins are transmembrane cell-extracellular matrix adhesion receptors that impact many cellular functions. A subgroup of integrins contain an inserted (I) domain within the alpha-subunits (alphaI) that mediate ligand recognition where function is contingent on binding a divalent cation at the metal ion dependent adhesion site (MIDAS). Ca(2+) is reported to promote alpha1I but inhibit alpha2I ligand binding. We co-crystallized individual I-domains with MIDAS-bound Ca(2+) and report structures at 1.4 and 2.15 A resolution, respectively. Both structures are in the "closed" ligand binding conformation where Ca(2+) induces minimal global structural changes. Comparisons with Mg(2+)-bound structures reveal Mg(2+) and Ca(2+) bind alpha1I in a manner sufficient to promote ligand binding. In contrast, Ca(2+) is displaced in the alpha2I domain MIDAS by 1.4 A relative to Mg(2+) and unable to directly coordinate all MIDAS residues. We identified an E152-R192 salt bridge hypothesized to limit the flexibility of the alpha2I MIDAS, thus, reducing Ca(2+) binding. A alpha2I E152A construct resulted in a 10,000-fold increase in Mg(2+) and Ca(2+) binding affinity while increasing binding to collagen ligands 20%. These data indicate the E152-R192 salt bridge is a key distinction in the molecular mechanism of differential ion binding of these two I domains.
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Salt-bridge modulates differential calcium-mediated ligand binding to integrin alpha1- and alpha2-I domains.,Brown KL, Banerjee S, Feigley A, Abe H, Blackwell TS, Pozzi A, Hudson BG, Zent R Sci Rep. 2018 Feb 13;8(1):2916. doi: 10.1038/s41598-018-21231-1. PMID:29440721<ref>PMID:29440721</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5hgj" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Integrin 3D structures|Integrin 3D structures]]
*[[Integrin 3D structures|Integrin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Abe, H]]
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[[Category: Abe H]]
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[[Category: Banerjee, S]]
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[[Category: Banerjee S]]
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[[Category: Blackwell, T]]
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[[Category: Blackwell T]]
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[[Category: Brown, K L]]
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[[Category: Brown KL]]
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[[Category: Feigley, A]]
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[[Category: Feigley A]]
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[[Category: Hudson, B H]]
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[[Category: Hudson BH]]
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[[Category: Pozzi, A]]
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[[Category: Pozzi A]]
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[[Category: Zent, R]]
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[[Category: Zent R]]
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[[Category: Cell adhesion]]
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[[Category: I-domain]]
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[[Category: Integrin]]
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[[Category: Rossman]]
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[[Category: Signaling]]
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Current revision

Structure of integrin alpha1beta1 and alpha2beta1 I-domains explain differential calcium-mediated ligand recognition

PDB ID 5hgj

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