1w52

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[[Image:1w52.gif|left|200px]]
 
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==Crystal structure of a proteolyzed form of pancreatic lipase related protein 2 from horse==
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The line below this paragraph, containing "STRUCTURE_1w52", creates the "Structure Box" on the page.
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<StructureSection load='1w52' size='340' side='right'caption='[[1w52]], [[Resolution|resolution]] 2.99&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'>[[1w52]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W52 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]] 2.99&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DDQ:DECYLAMINE-N,N-DIMETHYL-N-OXIDE'>DDQ</scene></td></tr>
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{{STRUCTURE_1w52| PDB=1w52 | 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=1w52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w52 OCA], [https://pdbe.org/1w52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w52 RCSB], [https://www.ebi.ac.uk/pdbsum/1w52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w52 ProSAT]</span></td></tr>
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</table>
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'''CRYSTAL STRUCTURE OF A PROTEOLYZED FORM OF PANCREATIC LIPASE RELATED PROTEIN 2 FROM HORSE'''
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== Function ==
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[https://www.uniprot.org/uniprot/Q95KP4_HORSE Q95KP4_HORSE]
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== Evolutionary Conservation ==
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==Overview==
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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/w5/1w52_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=1w52 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 ==
Horse pancreatic lipase-related proteins PLRP1 and PLRP2 are produced by the pancreas together with pancreatic lipase (PL). Sequence-comparison analyses reveal that the three proteins possess the same two-domain organization: an N-terminal catalytic domain and a C-terminal domain, which in PL is involved in colipase binding. Nevertheless, despite the high level of sequence identity found, they exhibit distinct enzymatic properties. The intrinsic sensitivity of the peptide bond between Ser245 and Thr246 within the flap region of PLRP2 to proteolytic cleavage probably complicates PLRP2 crystallization since, as shown here, this proteolyzed form of PLRP2 is only crystallized after specific detergent stabilization of this region. This has been performed by the hanging-drop vapour-diffusion method at 291 K and exclusively in the presence of N,N-dimethyldecylamine-beta-oxide (DDAO). However, most crystals (&gt;95%) are highly twinned and diffract poorly (to approximately 7-5 A resolution). Diffraction-quality trigonal crystals have unit-cell parameters a = b = 128.4, c = 85.8 A and belong to space group P3(2)21. A 2.9 A native data set was collected at ESRF on beamline ID14-2 with an R(merge) of 12.7%. Preliminary structural analysis provides a structural basis for the specific roles of DDAO.
Horse pancreatic lipase-related proteins PLRP1 and PLRP2 are produced by the pancreas together with pancreatic lipase (PL). Sequence-comparison analyses reveal that the three proteins possess the same two-domain organization: an N-terminal catalytic domain and a C-terminal domain, which in PL is involved in colipase binding. Nevertheless, despite the high level of sequence identity found, they exhibit distinct enzymatic properties. The intrinsic sensitivity of the peptide bond between Ser245 and Thr246 within the flap region of PLRP2 to proteolytic cleavage probably complicates PLRP2 crystallization since, as shown here, this proteolyzed form of PLRP2 is only crystallized after specific detergent stabilization of this region. This has been performed by the hanging-drop vapour-diffusion method at 291 K and exclusively in the presence of N,N-dimethyldecylamine-beta-oxide (DDAO). However, most crystals (&gt;95%) are highly twinned and diffract poorly (to approximately 7-5 A resolution). Diffraction-quality trigonal crystals have unit-cell parameters a = b = 128.4, c = 85.8 A and belong to space group P3(2)21. A 2.9 A native data set was collected at ESRF on beamline ID14-2 with an R(merge) of 12.7%. Preliminary structural analysis provides a structural basis for the specific roles of DDAO.
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==About this Structure==
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Crystallization of a proteolyzed form of the horse pancreatic lipase-related protein 2: structural basis for the specific detergent requirement.,Mancheno JM, Jayne S, Kerfelec B, Chapus C, Crenon I, Hermoso JA Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):2107-9. Epub 2004, Oct 20. PMID:15502342<ref>PMID:15502342</ref>
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1W52 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W52 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystallization of a proteolyzed form of the horse pancreatic lipase-related protein 2: structural basis for the specific detergent requirement., Mancheno JM, Jayne S, Kerfelec B, Chapus C, Crenon I, Hermoso JA, Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):2107-9. Epub 2004, Oct 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15502342 15502342]
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</div>
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<div class="pdbe-citations 1w52" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chapus, C.]]
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[[Category: Chapus C]]
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[[Category: Crenon, I.]]
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[[Category: Crenon I]]
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[[Category: Hermoso, J A.]]
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[[Category: Hermoso JA]]
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[[Category: Jayne, S.]]
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[[Category: Jayne S]]
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[[Category: Kerfelec, B.]]
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[[Category: Kerfelec B]]
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[[Category: Mancheno, J.]]
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[[Category: Mancheno JM]]
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[[Category: Cleaved flap]]
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[[Category: Detergent]]
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[[Category: Lipase]]
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[[Category: Pancreatic lipase related protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:10:11 2008''
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Current revision

Crystal structure of a proteolyzed form of pancreatic lipase related protein 2 from horse

PDB ID 1w52

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