1hs6
From Proteopedia
(New page: 200px<br /> <applet load="1hs6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hs6, resolution 1.95Å" /> '''STRUCTURE OF LEUKOT...) |
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| - | [[Image:1hs6.gif|left|200px]]<br /> | + | [[Image:1hs6.gif|left|200px]]<br /><applet load="1hs6" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hs6" size=" | + | |
caption="1hs6, resolution 1.95Å" /> | caption="1hs6, resolution 1.95Å" /> | ||
'''STRUCTURE OF LEUKOTRIENE A4 HYDROLASE COMPLEXED WITH BESTATIN.'''<br /> | '''STRUCTURE OF LEUKOTRIENE A4 HYDROLASE COMPLEXED WITH BESTATIN.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Leukotriene (LT) A(4) hydrolase/aminopeptidase (LTA4H) is a bifunctional | + | Leukotriene (LT) A(4) hydrolase/aminopeptidase (LTA4H) is a bifunctional zinc enzyme that catalyzes the biosynthesis of LTB4, a potent lipid chemoattractant involved in inflammation, immune responses, host defense against infection, and PAF-induced shock. The high resolution crystal structure of LTA4H in complex with the competitive inhibitor bestatin reveals a protein folded into three domains that together create a deep cleft harboring the catalytic Zn(2+) site. A bent and narrow pocket, shaped to accommodate the substrate LTA(4), constitutes a highly confined binding region that can be targeted in the design of specific anti-inflammatory agents. Moreover, the structure of the catalytic domain is very similar to that of thermolysin and provides detailed insight into mechanisms of catalysis, in particular the chemical strategy for the unique epoxide hydrolase reaction that generates LTB(4). |
==About this Structure== | ==About this Structure== | ||
| - | 1HS6 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 ZN, YB, ACT, BES and IMD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Leukotriene-A(4)_hydrolase Leukotriene-A(4) hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.6 3.3.2.6] Full crystallographic information is available from [http:// | + | 1HS6 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=ZN:'>ZN</scene>, <scene name='pdbligand=YB:'>YB</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=BES:'>BES</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Leukotriene-A(4)_hydrolase Leukotriene-A(4) hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.6 3.3.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HS6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Leukotriene-A(4) hydrolase]] | [[Category: Leukotriene-A(4) hydrolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Haeggstrom, J | + | [[Category: Haeggstrom, J Z.]] |
| - | [[Category: Nordlund, P | + | [[Category: Nordlund, P N.]] |
| - | [[Category: Thunnissen, M | + | [[Category: Thunnissen, M M.G M.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: BES]] | [[Category: BES]] | ||
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[[Category: protein-inhibitor complex]] | [[Category: protein-inhibitor complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:25 2008'' |
Revision as of 11:04, 21 February 2008
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STRUCTURE OF LEUKOTRIENE A4 HYDROLASE COMPLEXED WITH BESTATIN.
Overview
Leukotriene (LT) A(4) hydrolase/aminopeptidase (LTA4H) is a bifunctional zinc enzyme that catalyzes the biosynthesis of LTB4, a potent lipid chemoattractant involved in inflammation, immune responses, host defense against infection, and PAF-induced shock. The high resolution crystal structure of LTA4H in complex with the competitive inhibitor bestatin reveals a protein folded into three domains that together create a deep cleft harboring the catalytic Zn(2+) site. A bent and narrow pocket, shaped to accommodate the substrate LTA(4), constitutes a highly confined binding region that can be targeted in the design of specific anti-inflammatory agents. Moreover, the structure of the catalytic domain is very similar to that of thermolysin and provides detailed insight into mechanisms of catalysis, in particular the chemical strategy for the unique epoxide hydrolase reaction that generates LTB(4).
About this Structure
1HS6 is a Single protein structure of sequence from Homo sapiens with , , , and as ligands. Active as Leukotriene-A(4) hydrolase, with EC number 3.3.2.6 Full crystallographic information is available from OCA.
Reference
Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation., Thunnissen MM, Nordlund P, Haeggstrom JZ, Nat Struct Biol. 2001 Feb;8(2):131-5. PMID:11175901
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