3m3w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:31, 20 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3m3w' size='340' side='right'caption='[[3m3w]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3m3w' size='340' side='right'caption='[[3m3w]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3m3w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M3W FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3m3w]] is a 2 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=3M3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M3W 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=3m3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m3w OCA], [https://pdbe.org/3m3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m3w RCSB], [https://www.ebi.ac.uk/pdbsum/3m3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m3w 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]] 2.6&#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=3m3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m3w OCA], [https://pdbe.org/3m3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m3w RCSB], [https://www.ebi.ac.uk/pdbsum/3m3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m3w ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/PACN3_MOUSE PACN3_MOUSE]] Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity.
+
[https://www.uniprot.org/uniprot/PACN3_MOUSE PACN3_MOUSE] Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity.
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
BAR (Bin/amphiphysin/Rvs) domain-containing proteins participate in cellular membrane remodeling. The F-BAR proteins normally generate low-curvature tubules. However, in the PACSIN subfamily, the F-BAR domain from PACSIN 1 and 2 can induce both high- and low-curvature tubules. We found that unlike PACSIN 1 and 2, the PACSIN 3 could only induce low-curvature tubules. To elucidate the key factors that dictate the tubule curvature, crystal structures of all three PACSINs F-BAR domains were determined. A novel type of lateral interaction mediated by a wedge loop is observed between the F-BAR neighboring dimers. Comparisons of the structures of PACSIN 3 with PACSIN 1 and 2 indicate that the wedge loop of PACSIN 3 is more rigid, which influences the lateral interactions between assembled dimers. We further identified the residues that affect the rigidity of the loop by mutagenesis and determined the structures of two PACSIN 3 wedge loop mutants. Our results suggest that the rigidity-mediated conformations of the wedge loop correlate well with the various crystal packing modes and membrane tubulations. Thus, the rigidity of the wedge loop is a key factor in dictating tubule diameters.
+
-
 
+
-
The rigidity of the wedge loop in PACSIN 3 is a key factor in dictating the diameters of tubules.,Bai X, Meng G, Luo M, Zheng X J Biol Chem. 2012 May 9. PMID:22573331<ref>PMID:22573331</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3m3w" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Lk3 transgenic mice]]
+
[[Category: Mus musculus]]
-
[[Category: Bai, X Y]]
+
[[Category: Bai XY]]
-
[[Category: Meng, G]]
+
[[Category: Meng G]]
-
[[Category: Bar domain]]
+
-
[[Category: Endocytosis]]
+
-
[[Category: Mouse]]
+
-
[[Category: Pacsin3]]
+

Current revision

Crystal structure of mouse PACSIN3 BAR domain mutant

PDB ID 3m3w

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3m3w"
Personal tools