2pa1: Difference between revisions

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<StructureSection load='2pa1' size='340' side='right'caption='[[2pa1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2pa1' size='340' side='right'caption='[[2pa1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2pa1]] is a 1 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=2PA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PA1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2pa1]] is a 1 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=2PA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PA1 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></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]] 1.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDLIM2, PP6345 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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></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=2pa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pa1 OCA], [https://pdbe.org/2pa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pa1 RCSB], [https://www.ebi.ac.uk/pdbsum/2pa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pa1 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=2pa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pa1 OCA], [https://pdbe.org/2pa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pa1 RCSB], [https://www.ebi.ac.uk/pdbsum/2pa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pa1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PDLI2_HUMAN PDLI2_HUMAN]] Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity.  
[https://www.uniprot.org/uniprot/PDLI2_HUMAN PDLI2_HUMAN] Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity.
== 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=2pa1 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=2pa1 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 2pa1" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[PDZ and LIM domain protein|PDZ and LIM domain protein]]
*[[PDZ and LIM domain protein|PDZ and LIM domain protein]]
== References ==
<references/>
__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: Papagrigoriou E]]
[[Category: Papagrigoriou, E]]
[[Category: Pike ACW]]
[[Category: Pike, A C.W]]
[[Category: Salah E]]
[[Category: Structural genomic]]
[[Category: Shrestha L]]
[[Category: Salah, E]]
[[Category: Sundstrom M]]
[[Category: Shrestha, L]]
[[Category: Turnbull AP]]
[[Category: Sundstrom, M]]
[[Category: Ugochukwu E]]
[[Category: Turnbull, A P]]
[[Category: Umeano C]]
[[Category: Ugochukwu, E]]
[[Category: Uppenberg J]]
[[Category: Umeano, C]]
[[Category: Weigelt J]]
[[Category: Uppenberg, J]]
[[Category: Von Delft F]]
[[Category: Weigelt, J]]
[[Category: Metal binding protein]]
[[Category: Pdz domain]]
[[Category: Sgc]]

Latest revision as of 12:08, 21 February 2024

Structure of the PDZ domain of human PDLIM2 bound to a C-terminal extension from human beta-tropomyosinStructure of the PDZ domain of human PDLIM2 bound to a C-terminal extension from human beta-tropomyosin

Structural highlights

2pa1 is a 1 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 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PDLI2_HUMAN Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2pa1, resolution 1.70Å

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