1dmt: Difference between revisions
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New page: left|200px<br /> <applet load="1dmt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dmt, resolution 2.1Å" /> '''STRUCTURE OF HUMAN N... |
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[[Image:1dmt.gif|left|200px]]<br /> | [[Image:1dmt.gif|left|200px]]<br /><applet load="1dmt" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1dmt" size=" | |||
caption="1dmt, resolution 2.1Å" /> | caption="1dmt, resolution 2.1Å" /> | ||
'''STRUCTURE OF HUMAN NEUTRAL ENDOPEPTIDASE COMPLEXED WITH PHOSPHORAMIDON'''<br /> | '''STRUCTURE OF HUMAN NEUTRAL ENDOPEPTIDASE COMPLEXED WITH PHOSPHORAMIDON'''<br /> | ||
==Overview== | ==Overview== | ||
Neutral endopeptidase is a mammalian type II integral membrane | Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides. The range of substrates cleaved by neutral endopeptidase in vitro includes the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor. Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents. Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution. The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site. The inhibitor is bound to one side of this cavity and its binding mode provides a detailed understanding of the ligand-binding and specificity determinants. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1DMT 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 NAG, ZN, RDF and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Neprilysin Neprilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.11 3.4.24.11] Full crystallographic information is available from [http:// | 1DMT 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=NAG:'>NAG</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=RDF:'>RDF</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Neprilysin Neprilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.11 3.4.24.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Neprilysin]] | [[Category: Neprilysin]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Arcy, A | [[Category: Arcy, A D.]] | ||
[[Category: Dale, G | [[Category: Dale, G E.]] | ||
[[Category: Hennig, M.]] | [[Category: Hennig, M.]] | ||
[[Category: Oefner, C.]] | [[Category: Oefner, C.]] | ||
[[Category: Winkler, F | [[Category: Winkler, F K.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
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[[Category: signal-anchor]] | [[Category: signal-anchor]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:16 2008'' | ||
