3utl: Difference between revisions
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[[ | ==Human pepsin 3b== | ||
<StructureSection load='3utl' size='340' side='right' caption='[[3utl]], [[Resolution|resolution]] 2.61Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3utl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UTL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UTL FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pepsin_A Pepsin A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.1 3.4.23.1] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3utl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3utl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3utl RCSB], [http://www.ebi.ac.uk/pdbsum/3utl PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The analysis reported here describes detailed structural studies of endothiapepsin (the aspartic proteinase from Endothia parasitica), with and without bound inhibitors, and human pepsin 3b. Comparison of multiple crystal structures of members of the aspartic proteinase family has revealed small but significant differences in domain orientation in different crystal forms. In this paper, it is shown that these differences in domain orientation do not necessarily correlate with the presence or absence of bound inhibitors, but appear to stem at least partly from crystal contacts mediated by sulfate ions. However, since the same inherent flexibility of the structure is observed for other enzymes in this family such as human pepsin, the native structure of which is also reported here, the observed domain movements may well have implications for the mechanism of catalysis. | |||
An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases.,Bailey D, Carpenter EP, Coker A, Coker S, Read J, Jones AT, Erskine P, Aguilar CF, Badasso M, Toldo L, Rippmann F, Sanz-Aparicio J, Albert A, Blundell TL, Roberts NB, Wood SP, Cooper JB Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):541-52. Epub 2012 Apr 17. PMID:22525752<ref>PMID:22525752</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Pepsin|Pepsin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Pepsin A]] | [[Category: Pepsin A]] | ||
Revision as of 08:47, 5 June 2014
Human pepsin 3bHuman pepsin 3b
Structural highlights
Publication Abstract from PubMedThe analysis reported here describes detailed structural studies of endothiapepsin (the aspartic proteinase from Endothia parasitica), with and without bound inhibitors, and human pepsin 3b. Comparison of multiple crystal structures of members of the aspartic proteinase family has revealed small but significant differences in domain orientation in different crystal forms. In this paper, it is shown that these differences in domain orientation do not necessarily correlate with the presence or absence of bound inhibitors, but appear to stem at least partly from crystal contacts mediated by sulfate ions. However, since the same inherent flexibility of the structure is observed for other enzymes in this family such as human pepsin, the native structure of which is also reported here, the observed domain movements may well have implications for the mechanism of catalysis. An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases.,Bailey D, Carpenter EP, Coker A, Coker S, Read J, Jones AT, Erskine P, Aguilar CF, Badasso M, Toldo L, Rippmann F, Sanz-Aparicio J, Albert A, Blundell TL, Roberts NB, Wood SP, Cooper JB Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):541-52. Epub 2012 Apr 17. PMID:22525752[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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