1d7m: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1d7m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D7M FirstGlance]. <br>
<table><tr><td colspan='2'>[[1d7m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D7M FirstGlance]. <br>
</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=1d7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d7m OCA], [https://pdbe.org/1d7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d7m RCSB], [https://www.ebi.ac.uk/pdbsum/1d7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d7m ProSAT]</span></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]] 2.7&#8491;</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=1d7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d7m OCA], [https://pdbe.org/1d7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d7m RCSB], [https://www.ebi.ac.uk/pdbsum/1d7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d7m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/CTXA_DICDI CTXA_DICDI] Acting-bundling protein. When linked to F-actin the actin filaments form preferentially anti-parallel bundles that associate into meshworks. Plays a major role in cytokinesis. Negatively regulates cortical localization of rapgap1.<ref>PMID:18039932</ref>  
[https://www.uniprot.org/uniprot/CTXA_DICDI CTXA_DICDI] Acting-bundling protein. When linked to F-actin the actin filaments form preferentially anti-parallel bundles that associate into meshworks. Plays a major role in cytokinesis. Negatively regulates cortical localization of rapgap1.<ref>PMID:18039932</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: The parallel two-stranded alpha-helical coiled coil is the most frequently encountered subunit-oligomerization motif in proteins. The simplicity and regularity of this motif have made it an attractive system to explore some of the fundamental principles of protein folding and stability and to test the principles of de novo design. RESULTS: The X-ray crystal structure of the 18-heptad-repeat alpha-helical coiled-coil domain of the actin-bundling protein cortexillin I from Dictyostelium discoideum is a tightly packed parallel two-stranded alpha-helical coiled coil. It harbors a distinct 14-residue sequence motif that is essential for coiled-coil formation, and is a prerequisite for the assembly of cortexillin I. The atomic structure reveals novel types of ionic coiled-coil interactions. In particular, the structure shows that a characteristic interhelical and intrahelical salt-bridge pattern, in combination with the hydrophobic interactions occurring at the dimer interface, is the key structural feature of its coiled-coil trigger site. CONCLUSIONS: The knowledge gained from the structure could be used in the de novo design of alpha-helical coiled coils for applications such as two-stage drug targeting and delivery systems, and in the design of coiled coils as templates for combinatorial helical libraries in drug discovery and as synthetic carrier molecules.
The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges.,Burkhard P, Kammerer RA, Steinmetz MO, Bourenkov GP, Aebi U Structure. 2000 Mar 15;8(3):223-30. PMID:10745004<ref>PMID:10745004</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1d7m" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 06:50, 7 February 2024

COILED-COIL DIMERIZATION DOMAIN FROM CORTEXILLIN I

1d7m, resolution 2.70Å

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