1pir
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1pir.gif|left|200px]] | [[Image:1pir.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1pir", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1pir| PDB=1pir | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2''' | '''SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2''' | ||
| Line 23: | Line 20: | ||
==Reference== | ==Reference== | ||
Solution structure of porcine pancreatic phospholipase A2., van den Berg B, Tessari M, de Haas GH, Verheij HM, Boelens R, Kaptein R, EMBO J. 1995 Sep 1;14(17):4123-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7556053 7556053] | Solution structure of porcine pancreatic phospholipase A2., van den Berg B, Tessari M, de Haas GH, Verheij HM, Boelens R, Kaptein R, EMBO J. 1995 Sep 1;14(17):4123-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7556053 7556053] | ||
| - | [[Category: Phospholipase A(2)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
| Line 32: | Line 28: | ||
[[Category: Tessari, M.]] | [[Category: Tessari, M.]] | ||
[[Category: Verheij, H M.]] | [[Category: Verheij, H M.]] | ||
| - | [[Category: | + | [[Category: Phosphatide-2-acyl-hydrolase]] |
| - | [[Category: | + | [[Category: Phospholipase a2]] |
| - | [[Category: | + | [[Category: Pla2]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:07:40 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:07, 3 May 2008
SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2
Overview
The lipolytic enzyme phospholipase A2 (PLA2) is involved in the degradation of high-molecular weight phospholipid aggregates in vivo. The enzyme has very high catalytic activities on aggregated substrates compared with monomeric substrates, a phenomenon called interfacial activation. Crystal structures of PLA2s in the absence and presence of inhibitors are identical, from which it has been concluded that enzymatic conformational changes do not play a role in the mechanism of interfacial activation. The high-resolution NMR structure of porcine pancreatic PLA2 free in solution was determined with heteronuclear multidimensional NMR methodology using doubly labeled 13C, 15N-labeled protein. The solution structure of PLA2 shows important deviations from the crystal structure. In the NMR structure the Ala1 alpha-amino group is disordered and the hydrogen bonding network involving the N-terminus and the active site is incomplete. The disorder observed for the N-terminal region of PLA2 in the solution structure could be related to the low activity of the enzyme towards monomeric substrates. The NMR structure of PLA2 suggests, in contrast to the crystallographic work, that conformational changes do play a role in the interfacial activation of this enzyme.
About this Structure
1PIR is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Solution structure of porcine pancreatic phospholipase A2., van den Berg B, Tessari M, de Haas GH, Verheij HM, Boelens R, Kaptein R, EMBO J. 1995 Sep 1;14(17):4123-31. PMID:7556053 Page seeded by OCA on Sat May 3 05:07:40 2008
