1pb5

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[[Image:1pb5.png|left|200px]]
 
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==NMR Structure of a Prototype LNR Module from Human Notch1==
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The line below this paragraph, containing "STRUCTURE_1pb5", creates the "Structure Box" on the page.
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<StructureSection load='1pb5' size='340' side='right'caption='[[1pb5]]' 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'>[[1pb5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PB5 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">Solution NMR, 16 models</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=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_1pb5| PDB=1pb5 | 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=1pb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pb5 OCA], [https://pdbe.org/1pb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pb5 RCSB], [https://www.ebi.ac.uk/pdbsum/1pb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pb5 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/NOTC1_HUMAN NOTC1_HUMAN] Defects in NOTCH1 are a cause of aortic valve disease 1 (AOVD1) [MIM:[https://omim.org/entry/109730 109730]. A common defect in the aortic valve in which two rather than three leaflets are present. It is often associated with aortic valve calcification and insufficiency. In extreme cases, the blood flow may be so restricted that the left ventricle fails to grow, resulting in hypoplastic left heart syndrome.<ref>PMID:16025100</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/NOTC1_HUMAN NOTC1_HUMAN] Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. May be important for normal lymphocyte function. In altered form, may contribute to transformation or progression in some T-cell neoplasms. Involved in the maturation of both CD4+ and CD8+ cells in the thymus. May be important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, may function as a receptor for neuronal DNER and may be involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May enhance HIF1A function by sequestering HIF1AN away from HIF1A (By similarity).
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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/pb/1pb5_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=1pb5 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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Notch1 is a member of a conserved family of large modular heterodimeric type 1 transmembrane receptors that control differentiation in multicellular animals. Receptor maturation is accompanied by a furin-dependent cleavage that converts the Notch1 precursor polypeptide into a heterodimer consisting of an extracellular ligand-binding subunit (NEC) and a transmembrane signaling subunit (NTM). Binding of a physiologic ligand to NEC induces signaling by triggering additional proteolytic cleavages in NTM, which allow its intracellular region to translocate to the nucleus where it participates in a transcriptional activation complex. In the absence of ligand, the three conserved LNR modules of the NEC subunit participate in maintaining the receptor in its resting conformation. Here, we report the solution structure of the first LNR module (LNR_A) of human Notch1, and identify residues of LNR_A perturbed by the presence of the adjacent module LNR_B. LNR_A is held together by a unique arrangement of three disulfide bonds and a single bound Ca(2+) ion, and adopts a novel fold that falls in the general class of irregular disulfide-bonded structures. Residues perturbed by the presence of the adjacent LNR_B module are predominantly hydrophobic, and lie on one face of the module. These studies represent an initial step toward understanding the structural interrelationships among the three contiguous LNR modules required for proper regulation of Notch signaling.
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===NMR Structure of a Prototype LNR Module from Human Notch1===
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Nuclear magnetic resonance structure of a prototype Lin12-Notch repeat module from human Notch1.,Vardar D, North CL, Sanchez-Irizarry C, Aster JC, Blacklow SC Biochemistry. 2003 Jun 17;42(23):7061-7. PMID:12795601<ref>PMID:12795601</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_12795601}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1pb5" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12795601 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12795601}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1PB5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PB5 OCA].
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==Reference==
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Nuclear magnetic resonance structure of a prototype Lin12-Notch repeat module from human Notch1., Vardar D, North CL, Sanchez-Irizarry C, Aster JC, Blacklow SC, Biochemistry. 2003 Jun 17;42(23):7061-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12795601 12795601]
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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: Aster, J C.]]
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[[Category: Aster JC]]
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[[Category: Blacklow, S C.]]
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[[Category: Blacklow SC]]
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[[Category: North, C L.]]
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[[Category: North CL]]
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[[Category: Sanchez-Irizarry, C.]]
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[[Category: Sanchez-Irizarry C]]
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[[Category: Vardar, D.]]
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[[Category: Vardar D]]
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[[Category: Calcium-binding domain]]
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[[Category: Disulfide bond]]
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[[Category: Lin12/notch repeat]]
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[[Category: Notch signaling]]
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[[Category: Protein module]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:36:46 2008''
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Current revision

NMR Structure of a Prototype LNR Module from Human Notch1

PDB ID 1pb5

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