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==Structure of SH3 chimera with a type II ligand linked to the chain C-terminal== | ==Structure of SH3 chimera with a type II ligand linked to the chain C-terminal== | ||
<StructureSection load='3thk' size='340' side='right' caption='[[3thk]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3thk' size='340' side='right' caption='[[3thk]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3thk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3thk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2pqh 2pqh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3THK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3THK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <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">[[1pwt|1pwt]], [[1shg|1shg]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pwt|1pwt]], [[1shg|1shg]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sptan1, Spna2, Spta2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sptan1, Spna2, Spta2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3thk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3thk RCSB], [http://www.ebi.ac.uk/pdbsum/3thk PDBsum]</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=3thk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thk OCA], [http://pdbe.org/3thk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3thk RCSB], [http://www.ebi.ac.uk/pdbsum/3thk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3thk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/SPTN1_RAT SPTN1_RAT]] Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 19: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3thk" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 23: | Line 27: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Buffalo rat]] | ||
[[Category: Filimonov, V V]] | [[Category: Filimonov, V V]] | ||
[[Category: Gabdulkhakov, A G]] | [[Category: Gabdulkhakov, A G]] | ||
Revision as of 22:04, 10 December 2016
Structure of SH3 chimera with a type II ligand linked to the chain C-terminalStructure of SH3 chimera with a type II ligand linked to the chain C-terminal
Structural highlights
Function[SPTN1_RAT] Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Publication Abstract from PubMedA new chimeric protein, named WT-CIIA, was designed by connecting the proline-rich decapeptide PPPVPPYSAG to the C-terminus of the alpha-spectrin SH3 domain through a natural twelve-residue linker to obtain a single-chain model that would imitate intramolecular SH3-ligand interaction. The crystal structure of this fusion protein was determined at 1.7 A resolution. The asymmetric unit of the crystal contained two SH3 globules contacting with one PPPVPPY fragment located between them. The domains are related by the two-fold non-crystallographic axis and the ligand lies in two opposite orientations with respect to the conservative binding sites of SH3 domains. High-Resolution Crystal Structure of Spectrin SH3 Domain Fused with a Proline-Rich Peptide.,Gushchina LV, Gabdulkhakov AG, Nikonov SV, Filimonov VV J Biomol Struct Dyn. 2011 Dec;29(3):485-95. PMID:22066535[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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