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4nsw

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'''Unreleased structure'''
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==Crystal structure of the BAR-PH domain of ACAP1==
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<StructureSection load='4nsw' size='340' side='right' caption='[[4nsw]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4nsw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NSW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NSW FirstGlance]. <br>
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</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=4nsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nsw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nsw RCSB], [http://www.ebi.ac.uk/pdbsum/4nsw PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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The entry 4nsw is ON HOLD until Paper Publication
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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>
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Authors: Pang, X., Zhang, K., Ma, J., Zhou, Q., Sun, F.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure of the BAR-PH domain of ACAP1
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Ma, J.]]
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[[Category: Pang, X.]]
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[[Category: Sun, F.]]
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[[Category: Zhang, K.]]
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[[Category: Zhou, Q.]]
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[[Category: Bar domain]]
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[[Category: Coiled-coil]]
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[[Category: Gtpase activation]]
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[[Category: Membrane remodeling]]
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[[Category: Ph domain]]
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[[Category: Protein transport]]

Revision as of 10:46, 20 October 2014

Crystal structure of the BAR-PH domain of ACAP1

4nsw, resolution 2.20Å

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