4i1q

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==Crystal Structure of hBRAP1 N-BAR domain==
==Crystal Structure of hBRAP1 N-BAR domain==
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<StructureSection load='4i1q' size='340' side='right' caption='[[4i1q]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
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<StructureSection load='4i1q' size='340' side='right'caption='[[4i1q]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4i1q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I1Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4i1q]] is a 2 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=4I1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I1Q FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BIN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.53&#8491;</td></tr>
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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=4i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i1q RCSB], [http://www.ebi.ac.uk/pdbsum/4i1q PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4i1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i1q OCA], [https://pdbe.org/4i1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i1q RCSB], [https://www.ebi.ac.uk/pdbsum/4i1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i1q ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/BIN2_HUMAN BIN2_HUMAN] Promotes cell motility and migration, probably via its interaction with the cell membrane and with podosome proteins that mediate interaction with the cytoskeleton. Modulates membrane curvature and mediates membrane tubulation. Plays a role in podosome formation. Inhibits phagocytosis.<ref>PMID:23285027</ref>
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Cell motility, adhesion and phagocytosis are controlled by actin and membrane remodelling processes. Bridging integrator-2 (Bin2) also called Breast cancer-associated protein 1 (BRAP1) is a predicted N-BAR domain containing protein with unknown function that is highly expressed in leucocytic cells. In the present study we solved the structure of Bin2 BAR domain and studied its membrane binding and bending properties in vitro and in vivo. Live-cell imaging experiments showed that Bin2 is associated with actin rich structures on the plasma membrane, where it was targeted through its N-BAR domain. Pull-down experiments and immunoprecipitations showed that Bin2 C-terminus bound SH3 domain containing proteins such as Endophilin A2 and alpha-PIX. siRNA of endogenous protein led to decreased cell migration, increased phagocytosis and reduced podosome density and dynamics. In contrast, overexpression of Bin2 led to decreased phagocytosis and increased podosome density and dynamics. We conclude that Bin2 is a membrane-sculpting protein that influences podosome formation, motility and phagocytosis in leucocytes. Further understanding of this protein may be key to understand the behaviour of leucocytes under physiological and pathological conditions.
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Bin2 Is a Membrane Sculpting N-BAR Protein That Influences Leucocyte Podosomes, Motility and Phagocytosis.,Sanchez-Barrena MJ, Vallis Y, Clatworthy MR, Doherty GJ, Veprintsev DB, Evans PR, McMahon HT PLoS One. 2012;7(12):e52401. doi: 10.1371/journal.pone.0052401. Epub 2012 Dec 20. PMID:23285027<ref>PMID:23285027</ref>
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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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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Sanchez-Barrena, M J]]
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[[Category: Large Structures]]
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[[Category: Cell adhesion]]
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[[Category: Sanchez-Barrena MJ]]
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[[Category: N-bar membrane binding domain]]
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[[Category: Pix and endophilin a2]]
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Current revision

Crystal Structure of hBRAP1 N-BAR domain

PDB ID 4i1q

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