2iln: Difference between revisions

Revision as of 12:10, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2iln.png

Template:STRUCTURE 2iln

Crystal structure of the Bowman-Birk inhibitor from snail medic seeds in complex with bovine trypsinCrystal structure of the Bowman-Birk inhibitor from snail medic seeds in complex with bovine trypsin

Template:ABSTRACT PUBMED 17142058

About this StructureAbout this Structure

2ILN is a Protein complex structure of sequences from Bos taurus and Medicago scutellata. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the anticarcinogenic Bowman-Birk inhibitor from snail medic (Medicago scutellata) seeds complexed with bovine trypsin., Capaldi S, Perduca M, Faggion B, Carrizo ME, Tava A, Ragona L, Monaco HL, J Struct Biol. 2007 Apr;158(1):71-9. Epub 2006 Oct 26. PMID:17142058

Page seeded by OCA on Tue Jul 29 12:10:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of the Bowman-Birk inhibitor from snail medic seeds in complex with bovine trypsin'''
+===Crystal structure of the Bowman-Birk inhibitor from snail medic seeds in complex with bovine trypsin===
-==Overview==
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-The structure of the ternary complex of the anticarcinogenic Bowman-Birk protease inhibitor purified from snail medic (Medicago scutellata) seeds (MSTI) and two molecules of bovine trypsin has been solved by X-ray diffraction analysis of single crystals to a resolution of 2.0 A. This is the highest resolution model of a ternary complex of this type currently available. The two binding loops of the MSTI differ in only one amino acid and have in both cases an arginine in position P1. The distances between the residues of the inhibitor at the binding interface and the trypsin side chains that recognize them are almost identical in the two sites. When compared to the NMR model of the uncomplexed MSTI, the inhibitor in the functional assembly with trypsin shows the largest differences in the two P2' residues. Compared with the similar ternary complex of the soybean trypsin inhibitor, this model shows very small differences in the polypeptide chain of the trypsin binding sites and its largest difference in the area between Asp 26 and His 32 of the MSTI which in the soybean inhibitor has an extra Leu inserted in position 29.
+The line below this paragraph, {{ABSTRACT_PUBMED_17142058}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17142058 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17142058}}
 ==About this Structure==
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 [[Category: Protease inhibitor]]
 [[Category: Trypsin]]
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