4ag4: Difference between revisions
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==Crystal structure of a DDR1-Fab complex== | ==Crystal structure of a DDR1-Fab complex== | ||
<StructureSection load='4ag4' size='340' side='right' caption='[[4ag4]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='4ag4' size='340' side='right'caption='[[4ag4]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ag4]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ag4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AG4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id=' | <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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ag4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ag4 OCA], [https://pdbe.org/4ag4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ag4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ag4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ag4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/DDR1_HUMAN DDR1_HUMAN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 15: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ag4" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Monoclonal | *[[Epithelial discoidin domain-containing receptor|Epithelial discoidin domain-containing receptor]] | ||
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 23: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Carafoli F]] | |||
[[Category: Carafoli | [[Category: Chan LY]] | ||
[[Category: Chan | [[Category: Hohenester E]] | ||
[[Category: Hohenester | [[Category: Leitinger B]] | ||
[[Category: Leitinger | [[Category: Mayer MC]] | ||
[[Category: Mayer | [[Category: Nan R]] | ||
[[Category: Nan | [[Category: Pecheva MA]] | ||
[[Category: Pecheva | [[Category: Shiraishi K]] | ||
[[Category: Shiraishi | |||
Latest revision as of 14:26, 20 December 2023
Crystal structure of a DDR1-Fab complexCrystal structure of a DDR1-Fab complex
Structural highlights
FunctionPublication Abstract from PubMedThe discoidin domain receptors, DDR1 and DDR2, are constitutively dimeric receptor tyrosine kinases that are activated by triple-helical collagen. Aberrant DDR signaling contributes to several human pathologies, including many cancers. We have generated monoclonal antibodies (mAbs) that inhibit DDR1 signaling without interfering with collagen binding. The crystal structure of the monomeric DDR1 extracellular region bound to the Fab fragment of mAb 3E3 reveals that the collagen-binding discoidin (DS) domain is tightly associated with the following DS-like domain, which contains the epitopes of all mAbs. A conserved surface patch in the DS domain outside the collagen-binding site is shown to be required for signaling. Thus, the active conformation of the DDR1 dimer involves collagen-induced contacts between the DS domains, in addition to the previously identified association of transmembrane helices. The mAbs likely inhibit signaling by sterically blocking the extracellular association of DDR1 subunits. Structure of the discoidin domain receptor 1 extracellular region bound to an inhibitory fab fragment reveals features important for signaling.,Carafoli F, Mayer MC, Shiraishi K, Pecheva MA, Chan LY, Nan R, Leitinger B, Hohenester E Structure. 2012 Apr 4;20(4):688-97. Epub 2012 Apr 3. PMID:22483115[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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