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<StructureSection load='2q3g' size='340' side='right'caption='[[2q3g]], [[Resolution|resolution]] 1.11&Aring;' scene=''>
<StructureSection load='2q3g' size='340' side='right'caption='[[2q3g]], [[Resolution|resolution]] 1.11&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2q3g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q3G FirstGlance]. <br>
<table><tr><td colspan='2'>[[2q3g]] 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=2Q3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q3G FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.11&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2q3h|2q3h]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDLIM7 ([https://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=2q3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3g OCA], [https://pdbe.org/2q3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q3g RCSB], [https://www.ebi.ac.uk/pdbsum/2q3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q3g ProSAT]</span></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=2q3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3g OCA], [https://pdbe.org/2q3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q3g RCSB], [https://www.ebi.ac.uk/pdbsum/2q3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q3g ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PDLI7_HUMAN PDLI7_HUMAN]] May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity).<ref>PMID:7929196</ref> <ref>PMID:11874232</ref>
[https://www.uniprot.org/uniprot/PDLI7_HUMAN PDLI7_HUMAN] May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity).<ref>PMID:7929196</ref> <ref>PMID:11874232</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2q3g ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2q3g ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
PDZ domains most commonly bind the C-terminus of their protein targets. Typically the C-terminal four residues of the protein target are considered as the binding motif, particularly the C-terminal residue (P0) and third-last residue (P-2) that form the major contacts with the PDZ domain's "binding groove". We solved crystal structures of seven human PDZ domains, including five of the seven PDLIM family members. The structures of GRASP, PDLIM2, PDLIM5, and PDLIM7 show a binding mode with only the C-terminal P0 residue bound in the binding groove. Importantly, in some cases, the P-2 residue formed interactions outside of the binding groove, providing insight into the influence of residues remote from the binding groove on selectivity. In the GRASP structure, we observed both canonical and noncanonical binding in the two molecules present in the asymmetric unit making a direct comparison of these binding modes possible. In addition, structures of the PDZ domains from PDLIM1 and PDLIM4 also presented here allow comparison with canonical binding for the PDLIM PDZ domain family. Although influenced by crystal packing arrangements, the structures nevertheless show that changes in the positions of PDZ domain side-chains and the alpha B helix allow noncanonical binding interactions. These interactions may be indicative of intermediate states between unbound and fully bound PDZ domain and target protein. The noncanonical "perpendicular" binding observed potentially represents the general form of a kinetic intermediate. Comparison with canonical binding suggests that the rearrangement during binding involves both the PDZ domain and its ligand.
Unusual binding interactions in PDZ domain crystal structures help explain binding mechanisms.,Elkins JM, Gileadi C, Shrestha L, Phillips C, Wang J, Muniz JR, Doyle DA Protein Sci. 2010 Apr;19(4):731-41. doi: 10.1002/pro.349. PMID:20120020<ref>PMID:20120020</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2q3g" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bunkoczi, G]]
[[Category: Bunkoczi G]]
[[Category: Burgess-Brown, N]]
[[Category: Burgess-Brown N]]
[[Category: Delft, F von]]
[[Category: Doyle DA]]
[[Category: Doyle, D A]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Elkins J]]
[[Category: Elkins, J]]
[[Category: Gileadi C]]
[[Category: Gileadi, C]]
[[Category: Gileadi O]]
[[Category: Gileadi, O]]
[[Category: Papagrigoriou E]]
[[Category: Papagrigoriou, E]]
[[Category: Pike ACW]]
[[Category: Pike, A C.W]]
[[Category: Salah E]]
[[Category: Structural genomic]]
[[Category: Sundstrom M]]
[[Category: Salah, E]]
[[Category: Umeano C]]
[[Category: Sundstrom, M]]
[[Category: Uppenberg J]]
[[Category: Umeano, C]]
[[Category: Weigelt J]]
[[Category: Uppenberg, J]]
[[Category: Von Delft F]]
[[Category: Weigelt, J]]
[[Category: Sgc]]

Latest revision as of 09:14, 21 February 2024

Structure of the PDZ domain of human PDLIM7 bound to a C-terminal extension from human beta-tropomyosin

2q3g, resolution 1.11Å

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