4xbh: Difference between revisions
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==Soluble rabbit neprilysin== | ==Soluble rabbit neprilysin== | ||
<StructureSection load='4xbh' size='340' side='right' caption='[[4xbh]], [[Resolution|resolution]] 2.11Å' scene=''> | <StructureSection load='4xbh' size='340' side='right'caption='[[4xbh]], [[Resolution|resolution]] 2.11Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xbh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XBH FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xbh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XBH FirstGlance]. <br> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/NEP_RABIT NEP_RABIT]] Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.[UniProtKB:P08473] | [[http://www.uniprot.org/uniprot/NEP_RABIT NEP_RABIT]] Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.[UniProtKB:P08473] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Neutral endopeptidase (neprilysin; NEP) is a proteinase that cleaves a wide variety of peptides and has been implicated in Alzheimer's disease, cardiovascular conditions, arthritis and other inflammatory diseases. The structure of the soluble extracellular domain (residues 55-750) of rabbit neprilysin was solved both in its native form at 2.1 A resolution, and bound to the inhibitors phosphoramidon and thiorphan at 2.8 and 3.0 A resolution, respectively. Consistent with the extracellular domain of human neprilysin, the structure reveals a large central cavity which contains the active site and the location for inhibitor binding. | |||
Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan.,Labiuk SL, Sygusch J, Grochulski P Acta Crystallogr F Struct Biol Commun. 2019 Jun 1;75(Pt 6):405-411. doi:, 10.1107/S2053230X19006046. Epub 2019 May 10. PMID:31204686<ref>PMID:31204686</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4xbh" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Neprilysin|Neprilysin]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: European rabbit]] | [[Category: European rabbit]] | ||
[[Category: Large Structures]] | |||
[[Category: Neprilysin]] | [[Category: Neprilysin]] | ||
[[Category: Grochulski, P]] | [[Category: Grochulski, P]] | ||
Revision as of 10:18, 26 June 2019
Soluble rabbit neprilysinSoluble rabbit neprilysin
Structural highlights
Function[NEP_RABIT] Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers.[UniProtKB:P08473] Publication Abstract from PubMedNeutral endopeptidase (neprilysin; NEP) is a proteinase that cleaves a wide variety of peptides and has been implicated in Alzheimer's disease, cardiovascular conditions, arthritis and other inflammatory diseases. The structure of the soluble extracellular domain (residues 55-750) of rabbit neprilysin was solved both in its native form at 2.1 A resolution, and bound to the inhibitors phosphoramidon and thiorphan at 2.8 and 3.0 A resolution, respectively. Consistent with the extracellular domain of human neprilysin, the structure reveals a large central cavity which contains the active site and the location for inhibitor binding. Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan.,Labiuk SL, Sygusch J, Grochulski P Acta Crystallogr F Struct Biol Commun. 2019 Jun 1;75(Pt 6):405-411. doi:, 10.1107/S2053230X19006046. Epub 2019 May 10. PMID:31204686[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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