2akf: Difference between revisions

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<StructureSection load='2akf' size='340' side='right'caption='[[2akf]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
<StructureSection load='2akf' size='340' side='right'caption='[[2akf]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2akf]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AKF FirstGlance]. <br>
<table><tr><td colspan='2'>[[2akf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AKF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 1.2&#8491;</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=2akf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2akf OCA], [http://pdbe.org/2akf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2akf RCSB], [http://www.ebi.ac.uk/pdbsum/2akf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2akf ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2akf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2akf OCA], [https://pdbe.org/2akf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2akf RCSB], [https://www.ebi.ac.uk/pdbsum/2akf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2akf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/COR1A_MOUSE COR1A_MOUSE]] May be a crucial component of the cytoskeleton of highly motile cells, functioning both in the invagination of large pieces of plasma membrane, as well as in forming protrusions of the plasma membrane involved in cell locomotion. In mycobacteria-infected cells, its retention on the phagosomal membrane prevents fusion between phagosomes and lysosomes.<ref>PMID:10338208</ref> 
[https://www.uniprot.org/uniprot/COR1A_MOUSE COR1A_MOUSE] May be a crucial component of the cytoskeleton of highly motile cells, functioning both in the invagination of large pieces of plasma membrane, as well as in forming protrusions of the plasma membrane involved in cell locomotion. In mycobacteria-infected cells, its retention on the phagosomal membrane prevents fusion between phagosomes and lysosomes.<ref>PMID:10338208</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In recent years, short coiled coils have been used for applications ranging from biomaterial to medical sciences. For many of these applications knowledge of the factors that control the topology of the engineered protein systems is essential. Here, we demonstrate that trimerization of short coiled coils is determined by a distinct structural motif that encompasses specific networks of surface salt bridges and optimal hydrophobic packing interactions. The motif is conserved among intracellular, extracellular, viral, and synthetic proteins and defines a universal molecular determinant for trimer formation of short coiled coils. In addition to being of particular interest for the biotechnological production of candidate therapeutic proteins, these findings may be of interest for viral drug development strategies.
 
A conserved trimerization motif controls the topology of short coiled coils.,Kammerer RA, Kostrewa D, Progias P, Honnappa S, Avila D, Lustig A, Winkler FK, Pieters J, Steinmetz MO Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):13891-6. Epub 2005 Sep 19. PMID:16172398<ref>PMID:16172398</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2akf" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Avila, D]]
[[Category: Mus musculus]]
[[Category: Honnappa, S]]
[[Category: Avila D]]
[[Category: Kammerer, R A]]
[[Category: Honnappa S]]
[[Category: Kostrewa, D]]
[[Category: Kammerer RA]]
[[Category: Lustig, A]]
[[Category: Kostrewa D]]
[[Category: Pieters, J]]
[[Category: Lustig A]]
[[Category: Progias, P]]
[[Category: Pieters J]]
[[Category: Steinmetz, M O]]
[[Category: Progias P]]
[[Category: Winkler, F K]]
[[Category: Steinmetz MO]]
[[Category: Coiled coil]]
[[Category: Winkler FK]]
[[Category: Coronin 1]]
[[Category: Protein binding]]

Latest revision as of 13:41, 13 March 2024

Crystal structure of the coiled-coil domain of coronin 1

2akf, resolution 1.20Å

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