View source for 2fic


==The crystal structure of the BAR domain from human Bin1/Amphiphysin II and its implications for molecular recognition==
<StructureSection load='2fic' size='340' side='right'caption='[[2fic]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fic]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FIC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BIN1, AMPHL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2fic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fic OCA], [https://pdbe.org/2fic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fic RCSB], [https://www.ebi.ac.uk/pdbsum/2fic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fic ProSAT]</span></td></tr>
</table>
== Disease ==
[[https://www.uniprot.org/uniprot/BIN1_HUMAN BIN1_HUMAN]] Defects in BIN1 are the cause of centronuclear myopathy type 2 (CNM2) [MIM:[https://omim.org/entry/255200 255200]]. A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers.<ref>PMID:17676042</ref>  
== Function ==
[[https://www.uniprot.org/uniprot/BIN1_HUMAN BIN1_HUMAN]] May be involved in regulation of synaptic vesicle endocytosis. May act as a tumor suppressor and inhibits malignant cell transformation. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fi/2fic_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fic ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
BAR domains are found in proteins that bind and remodel membranes and participate in cytoskeletal and nuclear processes. Here, we report the crystal structure of the BAR domain from the human Bin1 protein at 2.0 A resolution. Both the quaternary and tertiary architectures of the homodimeric Bin1BAR domain are built upon "knobs-into-holes" packing of side chains, like those found in conventional left-handed coiled-coils, and this packing governs the curvature of a putative membrane-engaging concave face. Our calculations indicate that the Bin1BAR domain contains two potential sites for protein-protein interactions on the convex face of the dimer. Comparative analysis of structural features reveals that at least three architectural subtypes of the BAR domain are encoded in the human genome, represented by the Arfaptin, Bin1/Amphiphysin, and IRSp53 BAR domains. We discuss how these principal groups may differ in their potential to form regulatory heterotypic interactions.

The crystal structure of the BAR domain from human Bin1/amphiphysin II and its implications for molecular recognition.,Casal E, Federici L, Zhang W, Fernandez-Recio J, Priego EM, Miguel RN, DuHadaway JB, Prendergast GC, Luisi BF, Laue ED Biochemistry. 2006 Oct 31;45(43):12917-28. PMID:17059209<ref>PMID:17059209</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 2fic" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Casal, E]]
[[Category: Duhadaway, J B]]
[[Category: Federici, L]]
[[Category: Fernandez-Recio, J]]
[[Category: Laue, E D]]
[[Category: Luisi, B F]]
[[Category: Miguel, R N]]
[[Category: Prendergast, G C]]
[[Category: Priego, E M]]
[[Category: Zhang, W]]
[[Category: Bar domain]]
[[Category: Coiled-coil]]
[[Category: Endocytosis-exocytosis]]
[[Category: Endocytosis/exocytosis]]
[[Category: Homodimer]]
[[Category: Membrane protein complex]]