1w52
From Proteopedia
| Line 27: | Line 27: | ||
[[Category: pancreatic lipase related proteins]] | [[Category: pancreatic lipase related proteins]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:25:15 2007'' |
Revision as of 14:20, 30 October 2007
|
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, ... [(full description)]
About this Structure
1W52 is a [Single protein] structure of sequence from [Equus caballus] with CA and DDQ as [ligands]. Structure known Active Site: AC1. 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
Page seeded by OCA on Tue Oct 30 16:25:15 2007
