5p2p
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 5p2p |SIZE=350|CAPTION= <scene name='initialview01'>5p2p</scene>, resolution 2.4Å | |PDB= 5p2p |SIZE=350|CAPTION= <scene name='initialview01'>5p2p</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHG:PHOSPHONIC+ACID+2-DODECANOYLAMINO-HEXYL+ESTER+PROPYL+ESTER'>DHG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5p2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5p2p OCA], [http://www.ebi.ac.uk/pdbsum/5p2p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=5p2p RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Kalk, K H.]] | [[Category: Kalk, K H.]] | ||
[[Category: Thunnissen, M M.G M.]] | [[Category: Thunnissen, M M.G M.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: DHG]] | ||
[[Category: hydrolase(carboxylic ester)]] | [[Category: hydrolase(carboxylic ester)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:42:06 2008'' |
Revision as of 02:42, 31 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY STRUCTURE OF PHOSPHOLIPASE A2 COMPLEXED WITH A SUBSTRATE-DERIVED INHIBITOR
Overview
Phospholipases A2 play a part in a number of physiologically important cellular processes such as inflammation, blood platelet aggregation and acute hypersensitivity. These processes are all initiated by the release of arachidonic acid from cell membranes which is catalysed by intracellular phospholipases A2 and followed by conversion of arachidonic acid to prostaglandins, leukotrienes or thromboxanes. An imbalance in the production of these compounds can lead to chronic inflammatory diseases such as rheumatoid arthritis and asthma. Inhibitors of phospholipase A2 might therefore act to reduce the effects of inflammation, so structural information about the binding of phospholipase A2 to its substrates could be helpful in the design of therapeutic drugs. The three-dimensional structure is not known for any intracellular phospholipase A2, but these enzymes share significant sequence homology with secreted phospholipases, for which some of the structures have been determined. Here we report the structure of a complex between an extracellular phospholipase A2 and a competitively inhibiting substrate analogue, which reveals considerable detail about the interaction and suggests a mechanism for catalysis by this enzyme.
About this Structure
5P2P is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
X-ray structure of phospholipase A2 complexed with a substrate-derived inhibitor., Thunnissen MM, Ab E, Kalk KH, Drenth J, Dijkstra BW, Kuipers OP, Dijkman R, de Haas GH, Verheij HM, Nature. 1990 Oct 18;347(6294):689-91. PMID:2215698
Page seeded by OCA on Mon Mar 31 05:42:06 2008
