5xgg
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure C-terminal SH3 domain of Myosin IB from Entamoeba histolytica== | |
| + | <StructureSection load='5xgg' size='340' side='right' caption='[[5xgg]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5xgg]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XGG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XGG FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xg9|5xg9]]</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=5xgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xgg OCA], [http://pdbe.org/5xgg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xgg RCSB], [http://www.ebi.ac.uk/pdbsum/5xgg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xgg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The versatility in the recognition of various interacting proteins by the SH3 domain drives a variety of cellular functions. Here, the crystal structure of the C-terminal SH3 domain of myosin IB from Entamoeba histolytica (EhMySH3) is reported at a resolution of 1.7 A in native and PEG-bound states. Comparisons with other structures indicated that the PEG molecules occupy protein-protein interaction pockets similar to those occupied by the peptides in other peptide-bound SH3-domain structures. Also, analysis of the PEG-bound EhMySH3 structure led to the recognition of two additional pockets, apart from the conventional polyproline and specificity pockets, that are important for ligand interaction. Molecular-docking studies combined with various comparisons revealed structural similarity between EhMySH3 and the SH3 domain of beta-Pix, and this similarity led to the prediction that EhMySH3 preferentially binds targets containing type II-like PXXP motifs. These studies expand the understanding of the EhMySH3 domain and provide extensive structural knowledge, which is expected to help in predicting the interacting partners which function together with myosin IB during phagocytosis in E. histolytica infections. | ||
| - | + | Crystal structure of the PEG-bound SH3 domain of myosin IB from Entamoeba histolytica reveals its mode of ligand recognition.,Gautam G, Rehman SAA, Pandey P, Gourinath S Acta Crystallogr D Struct Biol. 2017 Aug 1;73(Pt 8):672-682. doi:, 10.1107/S2059798317009639. Epub 2017 Jul 28. PMID:28777082<ref>PMID:28777082</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5xgg" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Gautam, G]] | [[Category: Gautam, G]] | ||
| + | [[Category: Gourinath, S]] | ||
| + | [[Category: Contractile protein]] | ||
| + | [[Category: Ehmysh3]] | ||
| + | [[Category: Entamoeba histolytica]] | ||
| + | [[Category: Myosini]] | ||
| + | [[Category: Sh3]] | ||
Revision as of 06:00, 17 August 2017
Crystal Structure C-terminal SH3 domain of Myosin IB from Entamoeba histolytica
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