1mi1

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{{Seed}}
 
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[[Image:1mi1.png|left|200px]]
 
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==Crystal Structure of the PH-BEACH Domain of Human Neurobeachin==
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The line below this paragraph, containing "STRUCTURE_1mi1", creates the "Structure Box" on the page.
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<StructureSection load='1mi1' size='340' side='right'caption='[[1mi1]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1mi1]] 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=1MI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MI1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1mi1| PDB=1mi1 | SCENE= }}
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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=1mi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi1 OCA], [https://pdbe.org/1mi1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mi1 RCSB], [https://www.ebi.ac.uk/pdbsum/1mi1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mi1 ProSAT], [https://www.topsan.org/Proteins/NESGC/1mi1 TOPSAN]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mi/1mi1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1mi1 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The BEACH domain is highly conserved in a large family of eukaryotic proteins, and is crucial for their functions in vesicle trafficking, membrane dynamics and receptor signaling. However, it does not share any sequence homology with other proteins. Here we report the crystal structure at 2.9 A resolution of the BEACH domain of human neurobeachin. It shows that the BEACH domain has a new and unusual polypeptide backbone fold, as the peptide segments in its core do not assume regular secondary structures. Unexpectedly, the structure also reveals that the BEACH domain is in extensive association with a novel, weakly conserved pleckstrin-homology (PH) domain. Consistent with the structural analysis, biochemical studies show that the PH and BEACH domains have strong interactions, suggesting they may function as a single unit. Functional studies in intact cells demonstrate the requirement of both the PH and the BEACH domains for activity. A prominent groove at the interface between the two domains may be used to recruit their binding partners.
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===Crystal Structure of the PH-BEACH Domain of Human Neurobeachin===
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Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain.,Jogl G, Shen Y, Gebauer D, Li J, Wiegmann K, Kashkar H, Kronke M, Tong L EMBO J. 2002 Sep 16;21(18):4785-95. PMID:12234919<ref>PMID:12234919</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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The line below this paragraph, {{ABSTRACT_PUBMED_12234919}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1mi1" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12234919 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12234919}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1MI1 is a [[Single protein]] structure of 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=1MI1 OCA].
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==Reference==
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Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain., Jogl G, Shen Y, Gebauer D, Li J, Wiegmann K, Kashkar H, Kronke M, Tong L, EMBO J. 2002 Sep 16;21(18):4785-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12234919 12234919]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gebauer, D.]]
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[[Category: Gebauer D]]
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[[Category: Jogl, G.]]
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[[Category: Jogl G]]
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[[Category: Kashkar, H.]]
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[[Category: Kashkar H]]
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[[Category: Kroenke, M.]]
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[[Category: Kroenke M]]
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[[Category: Li, J.]]
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[[Category: Li J]]
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[[Category: NESG, Northeast Structural Genomics Consortium.]]
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[[Category: Shen Y]]
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[[Category: Shen, Y.]]
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[[Category: Tong L]]
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[[Category: Tong, L.]]
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[[Category: Wiegmann K]]
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[[Category: Wiegmann, K.]]
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[[Category: Beach domain]]
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[[Category: Nesg]]
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[[Category: Northeast structural genomics consortium]]
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[[Category: Ph domain]]
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[[Category: Protein structure initiative]]
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[[Category: Psi]]
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[[Category: Signal transduction]]
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[[Category: Structural genomic]]
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[[Category: Vesicle trafficking]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:00:51 2008''
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Current revision

Crystal Structure of the PH-BEACH Domain of Human Neurobeachin

PDB ID 1mi1

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