View source for 4ckh


==Helical reconstruction of ACAP1(BAR-PH domain) decorated membrane tubules by cryo-electron microscopy==
<SX load='4ckh' size='340' side='right' viewer='molstar' caption='[[4ckh]], [[Resolution|resolution]] 14.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ckh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CKH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 14&#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=4ckh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ckh OCA], [https://pdbe.org/4ckh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ckh RCSB], [https://www.ebi.ac.uk/pdbsum/4ckh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ckh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACAP1_HUMAN ACAP1_HUMAN] GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration.<ref>PMID:11062263</ref> <ref>PMID:16256741</ref> <ref>PMID:17398097</ref> <ref>PMID:17664335</ref> <ref>PMID:22645133</ref> 
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== Publication Abstract from PubMed ==
The BAR (Bin-Amphiphysin-Rvs) domain undergoes dimerization to produce a curved protein structure, which superimposes onto membrane through electrostatic interactions to sense and impart membrane curvature. In some cases, a BAR domain also possesses an amphipathic helix that inserts into the membrane to induce curvature. ACAP1 (Arfgap with Coil coil, Ankyrin repeat, and PH domain protein 1) contains a BAR domain. Here, we show that this BAR domain can neither bind membrane nor impart curvature, but instead requires a neighboring PH (Pleckstrin Homology) domain to achieve these functions. Specific residues within the PH domain are responsible for both membrane binding and curvature generation. The BAR domain adjacent to the PH domain instead interacts with the BAR domains of neighboring ACAP1 proteins to enable clustering at the membrane. Thus, we have uncovered the molecular basis for an unexpected and unconventional collaboration between PH and BAR domains in membrane bending.

A PH Domain in ACAP1 Possesses Key Features of the BAR Domain in Promoting Membrane Curvature.,Pang X, Fan J, Zhang Y, Zhang K, Gao B, Ma J, Li J, Deng Y, Zhou Q, Egelman EH, Hsu VW, Sun F Dev Cell. 2014 Oct 13;31(1):73-86. doi: 10.1016/j.devcel.2014.08.020. Epub 2014, Oct 2. PMID:25284369<ref>PMID:25284369</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4ckh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</SX>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Deng YC]]
[[Category: Fan J]]
[[Category: Gao BQ]]
[[Category: Hsu V]]
[[Category: Li J]]
[[Category: Ma J]]
[[Category: Pang XY]]
[[Category: Sun F]]
[[Category: Zhang K]]
[[Category: Zhang Y]]
[[Category: Zhou QJ]]