1sek

<table><tr><td colspan='2'>[[1sek]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Carolina_sphinx Carolina sphinx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SEK FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sek OCA], [https://pdbe.org/1sek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sek RCSB], [https://www.ebi.ac.uk/pdbsum/1sek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sek ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/SERA_MANSE SERA_MANSE]] Inhibits elastase.

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== Publication Abstract from PubMed ==

BACKGROUND: The reactive center loops (RCL) of serpins undergo large conformational changes triggered by the interaction with their target protease. Available crystallographic data suggest that the serpin RCL is polymorphic, but the relevance of the observed conformations to the competent active structure and the conformational changes that occur on binding target protease has remained obscure. New high-resolution data on an active serpin, serpin 1K from the moth hornworm Manduca sexta, provide insights into how active serpins are stabilized and how conformational changes are induced by protease binding. RESULTS: The 2.1 A structure shows that the RCL of serpin 1K, like that of active alpha1-antitrypsin, is canonical, complimentary and ready to bind to the target protease between P3 and P3 (where P refers to standard protease nomenclature),. In the hinge region (P17-P13), however, the RCL of serpin 1K, like ovalbumin and alpha1-antichymotrypsin, forms tight interactions that stabilize the five-stranded closed form of betasheet A. These interactions are not present in, and are not compatible with, the observed structure of active alpha1-antitrypsin. CONCLUSIONS: Serpin 1K may represent the best resting conformation for serpins - canonical near P1, but stabilized in the closed conformation of betasheet A. By comparison with other active serpins, especially alpha1-antitrypsin, a model is proposed in which interaction with the target protease near P1 leads to conformational changes in betasheet A of the serpin.

The structure of active serpin 1K from Manduca sexta.,Li J, Wang Z, Canagarajah B, Jiang H, Kanost M, Goldsmith EJ Structure. 1999 Jan 15;7(1):103-9. PMID:10368276<ref>PMID:10368276</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Carolina sphinx]]

[[Category: Canagarajah, B]]

[[Category: Goldsmith, E J]]

[[Category: Jiang, H]]

[[Category: Kanost, M]]

[[Category: Li, J]]

[[Category: Wang, Z]]

[[Category: Serpin]]