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| | ==The crystal structure of the second PDZ domain of human NHERF-2 (SLC9A3R2) interacting with a mode 1 PDZ binding motif== | | ==The crystal structure of the second PDZ domain of human NHERF-2 (SLC9A3R2) interacting with a mode 1 PDZ binding motif== |
| - | <StructureSection load='2he4' size='340' side='right' caption='[[2he4]], [[Resolution|resolution]] 1.45Å' scene=''> | + | <StructureSection load='2he4' size='340' side='right'caption='[[2he4]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2he4]] is a 1 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=2HE4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HE4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2he4]] 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=2HE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HE4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.45Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SLC9A3R2 ([http://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=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <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=2he4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2he4 OCA], [http://pdbe.org/2he4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2he4 RCSB], [http://www.ebi.ac.uk/pdbsum/2he4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2he4 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=2he4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2he4 OCA], [https://pdbe.org/2he4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2he4 RCSB], [https://www.ebi.ac.uk/pdbsum/2he4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2he4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NHRF2_HUMAN NHRF2_HUMAN]] Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus.<ref>PMID:9096337</ref> <ref>PMID:10455146</ref> | + | [https://www.uniprot.org/uniprot/NHRF2_HUMAN NHRF2_HUMAN] Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus.<ref>PMID:9096337</ref> <ref>PMID:10455146</ref> |
| | == 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: Arrowsmith, C]] | + | [[Category: Large Structures]] |
| - | [[Category: Berridge, G]] | + | [[Category: Arrowsmith C]] |
| - | [[Category: Bunkoczi, G]] | + | [[Category: Berridge G]] |
| - | [[Category: Colebrook, S]] | + | [[Category: Bunkoczi G]] |
| - | [[Category: Doyle, D A]] | + | [[Category: Colebrook S]] |
| - | [[Category: Edwards, A]] | + | [[Category: Doyle DA]] |
| - | [[Category: Elkins, J M]] | + | [[Category: Edwards A]] |
| - | [[Category: Gileadi, C]] | + | [[Category: Elkins JM]] |
| - | [[Category: Gileady, O]] | + | [[Category: Gileadi C]] |
| - | [[Category: Gorrec, F]] | + | [[Category: Gileady O]] |
| - | [[Category: Pantic, N]] | + | [[Category: Gorrec F]] |
| - | [[Category: Papagrigoriou, E]] | + | [[Category: Pantic N]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Papagrigoriou E]] |
| - | [[Category: Salah, E]] | + | [[Category: Salah E]] |
| - | [[Category: Savitsky, P]] | + | [[Category: Savitsky P]] |
| - | [[Category: Sundstrom, M]] | + | [[Category: Sundstrom M]] |
| - | [[Category: Weigelt, J]] | + | [[Category: Weigelt J]] |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Sgc]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
NHRF2_HUMAN Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus.[1] [2]
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
PDZ domains are protein-protein interaction modules that generally bind to the C termini of their target proteins. The C-terminal four amino acids of a prospective binding partner of a PDZ domain are typically the determinants of binding specificity. In an effort to determine the structures of a number of PDZ domains we have included appropriate four residue extensions on the C termini of PDZ domain truncation mutants, designed for self-binding. Multiple truncations of each PDZ domain were generated. The four residue extensions, which represent known specificity sequences of the target PDZ domains and cover both class I and II motifs, form intermolecular contacts in the expected manner for the interactions of PDZ domains with protein C termini for both classes. We present the structures of eight unique PDZ domains crystallized using this approach and focus on four which provide information on selectivity (PICK1 and the third PDZ domain of DLG2), binding site flexibility (the third PDZ domain of MPDZ), and peptide-domain interactions (MPDZ 12th PDZ domain). Analysis of our results shows a clear improvement in the chances of obtaining PDZ domain crystals by using this approach compared to similar truncations of the PDZ domains without the C-terminal four residue extensions.
Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions.,Elkins JM, Papagrigoriou E, Berridge G, Yang X, Phillips C, Gileadi C, Savitsky P, Doyle DA Protein Sci. 2007 Apr;16(4):683-94. PMID:17384233[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yun CH, Oh S, Zizak M, Steplock D, Tsao S, Tse CM, Weinman EJ, Donowitz M. cAMP-mediated inhibition of the epithelial brush border Na+/H+ exchanger, NHE3, requires an associated regulatory protein. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3010-5. PMID:9096337
- ↑ Zizak M, Lamprecht G, Steplock D, Tariq N, Shenolikar S, Donowitz M, Yun CH, Weinman EJ. cAMP-induced phosphorylation and inhibition of Na(+)/H(+) exchanger 3 (NHE3) are dependent on the presence but not the phosphorylation of NHE regulatory factor. J Biol Chem. 1999 Aug 27;274(35):24753-8. PMID:10455146
- ↑ Elkins JM, Papagrigoriou E, Berridge G, Yang X, Phillips C, Gileadi C, Savitsky P, Doyle DA. Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions. Protein Sci. 2007 Apr;16(4):683-94. PMID:17384233 doi:16/4/683
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