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| | ==Extending powder diffraction to proteins: structure solution of the second SH3 domain from ponsin== | | ==Extending powder diffraction to proteins: structure solution of the second SH3 domain from ponsin== |
| - | <StructureSection load='2o2w' size='340' side='right' caption='[[2o2w]]' scene=''> | + | <StructureSection load='2o2w' size='340' side='right'caption='[[2o2w]], [[Resolution|resolution]] 2.27Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2o2w]] 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=2O2W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O2W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2o2w]] 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=2O2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O2W FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o31|2o31]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray powder diffraction, [[Resolution|Resolution]] 2.27Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SORBS1 ([http://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=2o2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o2w OCA], [https://pdbe.org/2o2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o2w RCSB], [https://www.ebi.ac.uk/pdbsum/2o2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o2w ProSAT]</span></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=2o2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o2w OCA], [http://pdbe.org/2o2w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o2w RCSB], [http://www.ebi.ac.uk/pdbsum/2o2w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o2w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SRBS1_HUMAN SRBS1_HUMAN]] Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity).[UniProtKB:Q62417] | + | [https://www.uniprot.org/uniprot/SRBS1_HUMAN SRBS1_HUMAN] Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity).[UniProtKB:Q62417] |
| | == 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: Margiolaki, I]] | + | [[Category: Large Structures]] |
| - | [[Category: Pinotsis, N]] | + | [[Category: Margiolaki I]] |
| - | [[Category: Ponsin]] | + | [[Category: Pinotsis N]] |
| - | [[Category: Powder diffraction]]
| + | |
| - | [[Category: Sh3]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
SRBS1_HUMAN Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity).[UniProtKB:Q62417]
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
Determination of protein crystal structures is dependent on the growth of high-quality single crystals, a process that is not always successful. Optimum crystallization conditions must be systematically sought for, and microcrystalline powders are frequently obtained in failed attempts to grow the desired crystal. In materials science, structures of samples ranging from ceramics, pharmaceuticals, zeolites, etc., can nowadays be solved, almost routinely, from powdered samples, and there seems to be no fundamental reason, except the sheer size and complexity of the structures involved, why powder diffraction should not be employed to solve structures of small proteins. Indeed, recent work has shown that the high-quality powder diffraction data can be used in the study of protein crystal structures. We report the solution, model building, and refinement of a 67-residue protein domain crystal structure, with a cell volume of 64 879 A3, from powder diffraction. The second SH3 domain of ponsin, a protein of high biological significance due to its role in cellular processes, is determined and refined to resolution limits comparable to single-crystal techniques. Our results demonstrate the power and future applicability of the powder technique in structural biology.
Second SH3 domain of ponsin solved from powder diffraction.,Margiolaki I, Wright JP, Wilmanns M, Fitch AN, Pinotsis N J Am Chem Soc. 2007 Sep 26;129(38):11865-71. Epub 2007 Sep 5. PMID:17784760[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Margiolaki I, Wright JP, Wilmanns M, Fitch AN, Pinotsis N. Second SH3 domain of ponsin solved from powder diffraction. J Am Chem Soc. 2007 Sep 26;129(38):11865-71. Epub 2007 Sep 5. PMID:17784760 doi:10.1021/ja073846c
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