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3b7s
From Proteopedia
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[[Image:3b7s.png|left|200px]] | [[Image:3b7s.png|left|200px]] | ||
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{{STRUCTURE_3b7s| PDB=3b7s | SCENE= }} | {{STRUCTURE_3b7s| PDB=3b7s | SCENE= }} | ||
===[E296Q]LTA4H in complex with RSR substrate=== | ===[E296Q]LTA4H in complex with RSR substrate=== | ||
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==See Also== | ==See Also== | ||
| - | *[[Leukotriene A4 Hydrolase]] | + | *[[Leukotriene A4 Hydrolase|Leukotriene A4 Hydrolase]] |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:018804029</ref><ref group="xtra">PMID:017357161</ref><ref group="xtra">PMID:015078870</ref><ref group="xtra">PMID:011675384</ref><ref group="xtra">PMID:011917124</ref><ref group="xtra">PMID:011175901</ref><references group="xtra"/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Fournie-Zaluski, M C.]] | [[Category: Fournie-Zaluski, M C.]] | ||
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[[Category: Tholander, F.]] | [[Category: Tholander, F.]] | ||
[[Category: Thunnissen, M.]] | [[Category: Thunnissen, M.]] | ||
| - | [[Category: Alternative splicing]] | ||
[[Category: Analogue peptide]] | [[Category: Analogue peptide]] | ||
| - | [[Category: Cytoplasm]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Hydrolysis]] | [[Category: Hydrolysis]] | ||
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[[Category: Transition state]] | [[Category: Transition state]] | ||
[[Category: Tripeptide substrate]] | [[Category: Tripeptide substrate]] | ||
| - | [[Category: Zinc]] | ||
Revision as of 13:45, 26 July 2012
Contents |
[E296Q]LTA4H in complex with RSR substrate
Template:ABSTRACT PUBMED 18804029
About this Structure
3b7s is a 2 chain structure of Leukotriene A4 Hydrolase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Tholander F, Muroya A, Roques BP, Fournie-Zaluski MC, Thunnissen MM, Haeggstrom JZ. Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design. Chem Biol. 2008 Sep 22;15(9):920-9. PMID:18804029 doi:10.1016/j.chembiol.2008.07.018
- Tholander F, Haeggstrom JZ. Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase. Proteins. 2007 Jun 1;67(4):1113-8. PMID:17357161 doi:10.1002/prot.21329
- Rudberg PC, Tholander F, Andberg M, Thunnissen MM, Haeggstrom JZ. Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates. J Biol Chem. 2004 Jun 25;279(26):27376-82. Epub 2004 Apr 12. PMID:15078870 doi:10.1074/jbc.M401031200
- Rudberg PC, Tholander F, Thunnissen MM, Haeggstrom JZ. Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms. J Biol Chem. 2002 Jan 11;277(2):1398-404. Epub 2001 Oct 23. PMID:11675384 doi:10.1074/jbc.M106577200
- Rudberg PC, Tholander F, Thunnissen MM, Samuelsson B, Haeggstrom JZ. Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375. Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4215-20. Epub 2002 Mar 26. PMID:11917124 doi:10.1073/pnas.072090099
- Thunnissen MM, Nordlund P, Haeggstrom JZ. Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation. Nat Struct Biol. 2001 Feb;8(2):131-5. PMID:11175901 doi:10.1038/84117
Categories: Homo sapiens | Fournie-Zaluski, M C. | Haeggstrom, J. | Muroya, A. | Roques, B P. | Tholander, F. | Thunnissen, M. | Analogue peptide | Hydrolase | Hydrolysis | Leukotriene biosynthesis | Metal-binding | Metalloprotease | Multifunctional enzyme | Protease | Transition state | Tripeptide substrate
