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1d7m

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Revision as of 10:35, 14 December 2022

COILED-COIL DIMERIZATION DOMAIN FROM CORTEXILLIN I

Structural highlights

1d7m is a 2 chain structure with sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jeon TJ, Lee DJ, Lee S, Weeks G, Firtel RA. Regulation of Rap1 activity by RapGAP1 controls cell adhesion at the front of chemotaxing cells. J Cell Biol. 2007 Dec 3;179(5):833-43. Epub 2007 Nov 26. PMID:18039932 doi:jcb.200705068
↑ Burkhard P, Kammerer RA, Steinmetz MO, Bourenkov GP, Aebi U. The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges. Structure. 2000 Mar 15;8(3):223-30. PMID:10745004

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1d7m"

@@ Line 3: / Line 3: @@
 <StructureSection load='1d7m' size='340' side='right'caption='[[1d7m]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1d7m]] is a 2 chain structure. 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zta|2zta]]</div></td></tr>
+</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>
-<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>
 == 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 ==
@@ Line 22: / Line 21: @@
 __TOC__
 </StructureSection>
+[[Category: Dictyostelium discoideum]]
 [[Category: Large Structures]]
-[[Category: Aebi, U]]
+[[Category: Aebi U]]
-[[Category: Bourenkov, G P]]
+[[Category: Bourenkov GP]]
-[[Category: Burkhard, P]]
+[[Category: Burkhard P]]
-[[Category: Kammerer, R A]]
+[[Category: Kammerer RA]]
-[[Category: Steinmetz, M O]]
+[[Category: Steinmetz MO]]
-[[Category: Alpha helix]]
-[[Category: Coiled-coil]]
-[[Category: Coiled-coil trigger site]]
-[[Category: Contractile protein]]
-[[Category: Dimerization]]

1d7m

From Proteopedia

Revision as of 10:35, 14 December 2022

COILED-COIL DIMERIZATION DOMAIN FROM CORTEXILLIN I

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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