1w52
From Proteopedia
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| - | [[Image:1w52.gif|left|200px]]<br /> | + | [[Image:1w52.gif|left|200px]]<br /><applet load="1w52" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1w52" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1w52, resolution 2.99Å" /> | caption="1w52, resolution 2.99Å" /> | ||
'''CRYSTAL STRUCTURE OF A PROTEOLYZED FORM OF PANCREATIC LIPASE RELATED PROTEIN 2 FROM HORSE'''<br /> | '''CRYSTAL STRUCTURE OF A PROTEOLYZED FORM OF PANCREATIC LIPASE RELATED PROTEIN 2 FROM HORSE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W52 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with CA and DDQ as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 1W52 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with CA and DDQ as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Ca Binding Site For Chain X'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W52 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: pancreatic lipase related proteins]] | [[Category: pancreatic lipase related proteins]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:30:42 2007'' |
Revision as of 16:20, 18 December 2007
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CRYSTAL STRUCTURE OF A PROTEOLYZED FORM OF PANCREATIC LIPASE RELATED PROTEIN 2 FROM HORSE
Overview
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 (>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.
About this Structure
1W52 is a Single protein structure of sequence from Equus caballus with CA and DDQ as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
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