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4atm

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<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=4atm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4atm RCSB], [http://www.ebi.ac.uk/pdbsum/4atm PDBsum]</span></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=4atm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4atm RCSB], [http://www.ebi.ac.uk/pdbsum/4atm PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/AMPH_HUMAN AMPH_HUMAN]] May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton.
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</StructureSection>
</StructureSection>

Revision as of 11:45, 25 December 2014

Crystal structure of the BAR domain of human Amphiphysin, isoform 1 at 1.8 Angstrom resolution featuring increased order at the N- terminus.

4atm, resolution 1.78Å

Drag the structure with the mouse to rotate

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