1j37: Difference between revisions
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==Crystal Structure of Drosophila AnCE== | ==Crystal Structure of Drosophila AnCE== | ||
<StructureSection load='1j37' size='340' side='right' caption='[[1j37]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1j37' size='340' side='right'caption='[[1j37]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j37]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J37 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1j37]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J37 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J37 FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1j37" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1j37" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Angiotensin-Converting Enzyme 3D structures|Angiotensin-Converting Enzyme 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Drome]] | [[Category: Drome]] | ||
[[Category: Large Structures]] | |||
[[Category: Peptidyl-dipeptidase A]] | [[Category: Peptidyl-dipeptidase A]] | ||
[[Category: Kim, H M]] | [[Category: Kim, H M]] | ||
Revision as of 12:56, 30 October 2019
Crystal Structure of Drosophila AnCECrystal Structure of Drosophila AnCE
Structural highlights
Function[ACE_DROME] May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAngiotensin I-converting enzymes (ACEs) are zinc metallopeptidases that cleave carboxy-terminal dipeptides from short peptide hormones. We have determined the crystal structures of AnCE, a Drosophila homolog of ACE, with and without bound inhibitors to 2.4 A resolution. AnCE contains a large internal channel encompassing the entire protein molecule. This substrate-binding channel is composed of two chambers, reminiscent of a peanut shell. The inhibitor and zinc-binding sites are located in the narrow bottleneck connecting the two chambers. The substrate and inhibitor specificity of AnCE appears to be determined by extensive hydrogen-bonding networks and ionic interactions in the active site channel. The catalytically important zinc ion is coordinated by the conserved Glu395 and histidine residues from a HExxH motif. Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril.,Kim HM, Shin DR, Yoo OJ, Lee H, Lee JO FEBS Lett. 2003 Mar 13;538(1-3):65-70. PMID:12633854[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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