4xoj: Difference between revisions
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==Structure of bovine trypsin in complex with analogues of sunflower inhibitor 1 (SFTI-1)== | ==Structure of bovine trypsin in complex with analogues of sunflower inhibitor 1 (SFTI-1)== | ||
<StructureSection load='4xoj' size='340' side='right' caption='[[4xoj]], [[Resolution|resolution]] 0.91Å' scene=''> | <StructureSection load='4xoj' size='340' side='right'caption='[[4xoj]], [[Resolution|resolution]] 0.91Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xoj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XOJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XOJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xoj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XOJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XOJ FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4xoj" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4xoj" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Trypsin|Trypsin]] | |||
*[[Trypsin inhibitor|Trypsin inhibitor]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | |||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
[[Category: Brzozowski, K]] | [[Category: Brzozowski, K]] | ||
Revision as of 10:43, 4 March 2020
Structure of bovine trypsin in complex with analogues of sunflower inhibitor 1 (SFTI-1)Structure of bovine trypsin in complex with analogues of sunflower inhibitor 1 (SFTI-1)
Structural highlights
Function[SFTI1_HELAN] Inhibits trypsin, cathepsin G, elastase, chymotrypsin and thrombin. Does not inhibit factor Xa.[1] Publication Abstract from PubMedSerine proteinase catalyzed peptide splicing was demonstrated in both, one and two-peptide-chain (C- and N-terminal peptide chains linked by a disulfide bridge) trypsin inhibitor SFTI-1 analogues. In the second series, peptide splicing, with catalytic amount of proteinase, was observed only when formation of acyl-enzyme intermediate was preceded by the hydrolysis of the substrate Lys-Ser peptide bond. Here we presented that at an equimolar amount of the proteinase, splicing occurred in all two-peptide-chain analogues. This conclusion was supported by high resolution crystal structures of selected analogues in complex with trypsin. We showed that the process followed a direct transpeptidation mechanism. It means that the acyl-enzyme intermediate was formed and was immediately utilized for a new peptide bond formation, and products associated with the hydrolysis of acyl-enzyme were not observed. The demonstrated peptide splicing was a sequence- not structure-specific. Investigation of serine proteinase catalyzed peptide splicing in analogues of sunflower trypsin inhibitor 1 (SFTI-1).,Karna N, Malicki S, Debowski D, Golik P, Gitlin A, Grudnik P, Wladyka B, Brzozowski K, Dubin G, Rolka K, Legowska A Chembiochem. 2015 Jul 25. doi: 10.1002/cbic.201500296. PMID:26212347[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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