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New page: left|200px<br /> <applet load="1pod" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pod, resolution 2.1Å" /> '''STRUCTURES OF FREE A...
 
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[[Image:1pod.gif|left|200px]]<br />
[[Image:1pod.gif|left|200px]]<br /><applet load="1pod" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1pod" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1pod, resolution 2.1&Aring;" />
caption="1pod, resolution 2.1&Aring;" />
'''STRUCTURES OF FREE AND INHIBITED HUMAN SECRETORY PHOSPHOLIPASE A2 FROM INFLAMMATORY EXUDATE'''<br />
'''STRUCTURES OF FREE AND INHIBITED HUMAN SECRETORY PHOSPHOLIPASE A2 FROM INFLAMMATORY EXUDATE'''<br />


==Overview==
==Overview==
Phospholipase A2 (PLA2) participates in a wide range of cellular processes, including inflammation and transmembrane signaling. A human nonpancreatic, secretory PLA2 (hnps-PLA2) has been identified that is found in high, concentrations in the synovial fluid of patients with rheumatoid arthritis, and in the plasma of patients with septic shock. This enzyme is secreted, from certain cell types in response to the proinflammatory cytokines, tumor necrosis factor or interleukin-1. The crystal structures of the, calcium-bound form of this enzyme have been determined at physiological pH, both in the presence [2.1 angstrom (A) resolution] and absence (2.2 A, resolution) of a transition-state analogue. Although the critical features, that suggest the chemistry of catalysis are identical to those inferred, from the crystal structures of other extracellular PLA2s, the shape of the, hydrophobic channel of hnps-PLA2 is uniquely modulated by substrate, binding.
Phospholipase A2 (PLA2) participates in a wide range of cellular processes including inflammation and transmembrane signaling. A human nonpancreatic secretory PLA2 (hnps-PLA2) has been identified that is found in high concentrations in the synovial fluid of patients with rheumatoid arthritis and in the plasma of patients with septic shock. This enzyme is secreted from certain cell types in response to the proinflammatory cytokines, tumor necrosis factor or interleukin-1. The crystal structures of the calcium-bound form of this enzyme have been determined at physiological pH both in the presence [2.1 angstrom (A) resolution] and absence (2.2 A resolution) of a transition-state analogue. Although the critical features that suggest the chemistry of catalysis are identical to those inferred from the crystal structures of other extracellular PLA2s, the shape of the hydrophobic channel of hnps-PLA2 is uniquely modulated by substrate binding.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1POD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1POD OCA].  
1POD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POD OCA].  


==Reference==
==Reference==
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[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Scott, D.L.]]
[[Category: Scott, D L.]]
[[Category: Sigler, P.B.]]
[[Category: Sigler, P B.]]
[[Category: White, S.P.]]
[[Category: White, S P.]]
[[Category: CA]]
[[Category: CA]]
[[Category: hydrolase]]
[[Category: hydrolase]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:55 2008''

Revision as of 15:30, 21 February 2008

File:1pod.gif


1pod, resolution 2.1Å

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STRUCTURES OF FREE AND INHIBITED HUMAN SECRETORY PHOSPHOLIPASE A2 FROM INFLAMMATORY EXUDATE

OverviewOverview

Phospholipase A2 (PLA2) participates in a wide range of cellular processes including inflammation and transmembrane signaling. A human nonpancreatic secretory PLA2 (hnps-PLA2) has been identified that is found in high concentrations in the synovial fluid of patients with rheumatoid arthritis and in the plasma of patients with septic shock. This enzyme is secreted from certain cell types in response to the proinflammatory cytokines, tumor necrosis factor or interleukin-1. The crystal structures of the calcium-bound form of this enzyme have been determined at physiological pH both in the presence [2.1 angstrom (A) resolution] and absence (2.2 A resolution) of a transition-state analogue. Although the critical features that suggest the chemistry of catalysis are identical to those inferred from the crystal structures of other extracellular PLA2s, the shape of the hydrophobic channel of hnps-PLA2 is uniquely modulated by substrate binding.

DiseaseDisease

Known diseases associated with this structure: Colorectal cancer, sporadic OMIM:[172411]

About this StructureAbout this Structure

1POD is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

ReferenceReference

Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate., Scott DL, White SP, Browning JL, Rosa JJ, Gelb MH, Sigler PB, Science. 1991 Nov 15;254(5034):1007-10. PMID:1948070

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