1le6: Difference between revisions

Revision as of 13:16, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1le6.png

Template:STRUCTURE 1le6

CARBOXYLIC ESTER HYDROLASE, P 1 21 1 SPACE GROUPCARBOXYLIC ESTER HYDROLASE, P 1 21 1 SPACE GROUP

Template:ABSTRACT PUBMED 12161451

About this StructureAbout this Structure

1LE6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes., Pan YH, Yu BZ, Singer AG, Ghomashchi F, Lambeau G, Gelb MH, Jain MK, Bahnson BJ, J Biol Chem. 2002 Aug 9;277(32):29086-93. Epub 2002 May 25. PMID:12161451

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 {{STRUCTURE_1le6|  PDB=1le6  |  SCENE=  }}
-'''CARBOXYLIC ESTER HYDROLASE, P 1 21 1 SPACE GROUP'''
+===CARBOXYLIC ESTER HYDROLASE, P 1 21 1 SPACE GROUP===
-==Overview==
+<!--
-The crystal structure of human group X (hGX) secreted phospholipase A2 (sPLA2) has been solved to a resolution of 1.97 A. As expected the protein fold is similar to previously reported sPLA2 structures. The active site architecture, including the positions of the catalytic residues and the first and second shell water around the Ca2+ cofactor, are highly conserved and remarkably similar to the group IB and group IIA enzymes. Differences are seen in the structures following the (1-12)-N-terminal helix and at the C terminus. These regions are proposed to interact with the substrate membrane surface. The opening to the active site slot is considerably larger in hGX than in human group IIA sPLA2. Furthermore, the electrostatic surface potential of the hGX interfacial-binding surface does not resemble that of the human group IIA sPLA2; the former is highly neutral, whereas the latter is highly cationic. The cationic residues on this face of group IB and IIA enzymes have been implicated in membrane binding and in k(cat*) allostery. In contrast, hGX does not show activation by the anionic charge at the lipid interface when acting on phospholipid vesicles or short-chain phospholipid micelles. Together, the crystal structure and kinetic results of hGX supports the conclusion that it is as active on zwitterionic as on anionic interfaces, and thus it is predicted to target the zwitterionic membrane surfaces of mammalian cells.
+The line below this paragraph, {{ABSTRACT_PUBMED_12161451}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12161451}}
 ==About this Structure==
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 [[Category: Human phosphatidylcholine 2-acylhydrolase gx]]
 [[Category: Spla2-x]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:50:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 13:15:39 2008''