2ays: Difference between revisions
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==A conserved non-metallic binding site in the C-terminal lobe of lactoferrin: Structure of the complex of C-terminal lobe of bovine lactoferrin with N-acetyl galactosamine at 1.86 A resolution== | ==A conserved non-metallic binding site in the C-terminal lobe of lactoferrin: Structure of the complex of C-terminal lobe of bovine lactoferrin with N-acetyl galactosamine at 1.86 A resolution== | ||
<StructureSection load='2ays' size='340' side='right' caption='[[2ays]], [[Resolution|resolution]] 1.86Å' scene=''> | <StructureSection load='2ays' size='340' side='right'caption='[[2ays]], [[Resolution|resolution]] 1.86Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ays]] is a 1 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=2AYS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AYS FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ays]] is a 1 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=2AYS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AYS FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | |||
[[Category: Jabeen, T]] | [[Category: Jabeen, T]] | ||
[[Category: Sharma, S]] | [[Category: Sharma, S]] |
Revision as of 08:16, 13 February 2020
A conserved non-metallic binding site in the C-terminal lobe of lactoferrin: Structure of the complex of C-terminal lobe of bovine lactoferrin with N-acetyl galactosamine at 1.86 A resolutionA conserved non-metallic binding site in the C-terminal lobe of lactoferrin: Structure of the complex of C-terminal lobe of bovine lactoferrin with N-acetyl galactosamine at 1.86 A resolution
Structural highlights
Function[TRFL_BOVIN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.[1] [2] Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.[3] [4] Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.[5] [6] The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.[7] [8] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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