2p0m

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{{STRUCTURE_2p0m| PDB=2p0m | SCENE= }}
{{STRUCTURE_2p0m| PDB=2p0m | SCENE= }}
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'''Revised structure of rabbit reticulocyte 15S-lipoxygenase'''
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===Revised structure of rabbit reticulocyte 15S-lipoxygenase===
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==Overview==
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Lipoxygenases (LOXs) are a family of nonheme iron dioxygenases that catalyze the regioselective and stereospecific hydroperoxidation of polyunsaturated fatty acids, and are involved in a variety of inflammatory diseases and cancers. The crystal structure of rabbit 15S-LOX1 that was reported by Gillmor et al. in 1997 has played key roles for understanding the properties of mammalian LOXs. In this structure, three segments, including 12 residues in the superficial alpha2 helix, are absent and have usually been described as "disordered." By reinterpreting the original crystallographic data we were able to elucidate two different conformations of the molecule, both having well ordered alpha2 helices. Surprisingly, one molecule contained an inhibitor and the other did not, thereby adopting a closed and an open form, respectively. They differed in the conformation of the segments that were absent in the original structure, which is highlighted by a 12 A movement of alpha2. Consequently, they showed a difference in the size and shape of the substrate-binding cavity. The new model should provide new insight into the catalytic mechanism involving induced conformational change of the binding pocket. It may also be helpful for the structure-based design of LOX inhibitors.
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The line below this paragraph, {{ABSTRACT_PUBMED_17847087}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 17847087 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17847087}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data., Choi J, Chon JK, Kim S, Shin W, Proteins. 2008 Feb 15;70(3):1023-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17847087 17847087]
Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data., Choi J, Chon JK, Kim S, Shin W, Proteins. 2008 Feb 15;70(3):1023-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17847087 17847087]
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The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity., Gillmor SA, Villasenor A, Fletterick R, Sigal E, Browner MF, Nat Struct Biol. 1997 Dec;4(12):1003-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9406550 9406550]
[[Category: Arachidonate 15-lipoxygenase]]
[[Category: Arachidonate 15-lipoxygenase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Rabbit]]
[[Category: Rabbit]]
[[Category: Twin]]
[[Category: Twin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:04:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:20:34 2008''

Revision as of 10:20, 27 July 2008

Image:2p0m.png

Template:STRUCTURE 2p0m

Revised structure of rabbit reticulocyte 15S-lipoxygenase

Template:ABSTRACT PUBMED 17847087

About this Structure

2P0M is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data., Choi J, Chon JK, Kim S, Shin W, Proteins. 2008 Feb 15;70(3):1023-32. PMID:17847087

The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity., Gillmor SA, Villasenor A, Fletterick R, Sigal E, Browner MF, Nat Struct Biol. 1997 Dec;4(12):1003-9. PMID:9406550

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