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1ljv

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(New page: 200px<br /><applet load="1ljv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ljv" /> '''Bovine Pancreatic Polypeptide Bound to DPC M...)
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[[Image:1ljv.jpg|left|200px]]<br /><applet load="1ljv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ljv" />
 
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'''Bovine Pancreatic Polypeptide Bound to DPC Micelles'''<br />
 
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==Overview==
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==Bovine Pancreatic Polypeptide Bound to DPC Micelles==
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The pancreatic polypeptide (PP), a 36-residue, C-terminally amidated, polypeptide hormone is a member of the neuropeptide Y (NPY) family. Here, we have studied the structure and dynamics of bovine pancreatic, polypeptide (bPP) when bound to DPC-micelles as a membrane-mimicking model, as well as the dynamics of bPP in solution. The comparison of structure, and dynamics of bPP in both states reveals remarkable differences. The, overall correlation time of 5.08ns derived from the 15N relaxation data, proves unambiguously that bPP in solution exists as a dimer. Therein, intermolecular as well as intramolecular hydrophobic interactions from, residues of both the amphiphilic helix and of the back-folded N terminus, contribute to the stability of the PP fold. The overall rigidity is, well-reflected in positive values for the heteronuclear NOE for residues, 4-34.The membrane-bound species displays a partitioning into a more, flexible N-terminal region and a well-defined alpha-helical region, comprising residues 17-31. The average RMSD value for residues 17-31 is, 0.22(+/-0.09)A. The flexibility of the N terminus is compatible with, negative values of the heteronuclear NOE observed for the N-terminal, residues 4-12 and low values of the generalized order parameter S(2). The, membrane-peptide interface was investigated by micelle-integrating, spin-labels and H,2H exchange measurements. It is formed by those residues, which make contacts between the C-terminal alpha-helix and the polyproline, helix. In contrast to pNPY, also residues from the N terminus display, spatial proximity to the membrane interface. Furthermore, the orientation, of the C terminus, that presumably contains residues involved in receptor, binding, is different in the two environments. We speculate that this, pre-positioning of residues could be an important requirement for receptor, activation. Moreover, we doubt that the PP fold is of functional relevance, for binding at the Y(4) receptor.
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<StructureSection load='1ljv' size='340' side='right'caption='[[1ljv]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ljv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LJV FirstGlance]. <br>
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1LJV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LJV OCA].
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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</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=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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==Reference==
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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=1ljv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ljv OCA], [https://pdbe.org/1ljv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ljv RCSB], [https://www.ebi.ac.uk/pdbsum/1ljv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ljv ProSAT]</span></td></tr>
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Bovine pancreatic polypeptide (bPP) undergoes significant changes in conformation and dynamics upon binding to DPC micelles., Lerch M, Gafner V, Bader R, Christen B, Folkers G, Zerbe O, J Mol Biol. 2002 Oct 4;322(5):1117-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12367532 12367532]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PAHO_BOVIN PAHO_BOVIN] Pancreatic hormone is synthesized in pancreatic islets of Langerhans and acts as a regulator of pancreatic and gastrointestinal functions.
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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/lj/1ljv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ljv ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bader, R.]]
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[[Category: Bader R]]
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[[Category: Christen, B.]]
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[[Category: Christen B]]
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[[Category: Gafner, V.]]
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[[Category: Gafner V]]
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[[Category: Lerch, M.]]
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[[Category: Lerch M]]
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[[Category: Zerbe, O.]]
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[[Category: Zerbe O]]
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[[Category: NH2]]
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[[Category: nmr micelle peptide hormone]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:36:41 2007''
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Current revision

Bovine Pancreatic Polypeptide Bound to DPC Micelles

PDB ID 1ljv

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