1y3c: Difference between revisions

Revision as of 01:51, 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:1y3c.png

Template:STRUCTURE 1y3c

Crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 R62A mutantCrystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 R62A mutant

Template:ABSTRACT PUBMED 15865427

About this StructureAbout this Structure

1Y3C is a Protein complex structure of sequences from Bacillus amyloliquefaciens and Hordeum vulgare. Full crystallographic information is available from OCA.

ReferenceReference

Role of the intramolecular hydrogen bond network in the inhibitory power of chymotrypsin inhibitor 2., Radisky ES, Lu CJ, Kwan G, Koshland DE Jr, Biochemistry. 2005 May 10;44(18):6823-30. PMID:15865427

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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 complex of subtilisin BPN' with chymotrypsin inhibitor 2 R62A mutant'''
+===Crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 R62A mutant===
-==Overview==
+<!--
-A series of mutants of chymotrypsin inhibitor 2 (CI2), at residues involved in intramolecular interactions that shape and constrain the binding loop, were studied to determine their relative importance for inhibition of the serine protease subtilisin BPN', and for resistance of the inhibitor to proteolysis. These functional properties were investigated in tandem with the crystal structures of the mutant inhibitor-enzyme complexes. A dense hydrogen bonding network that supports the binding loop in the vicinity of the scissile bond was found to be important both for enzyme affinity and for stability to proteolysis. Structural analysis, in combination with biochemical measurements, allows differentiation of the structural components most important for resistance to proteolysis and/or binding. The most critical participating residues in the network were found to be Thr-58, Glu-60, Arg-65, and Gly-83. Glu-60 is more important for resistance to proteolysis than for binding, while Arg-65 and two other Arg residues play a greater role in binding than in resistance to proteolysis. Structural comparisons reveal a wide variety of subtle conformational changes in response to mutation, with built-in robustness in the hydrogen bond network, such that loss of one contact is compensated by other new contacts.
+The line below this paragraph, {{ABSTRACT_PUBMED_15865427}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15865427 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15865427}}
 ==About this Structure==
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 [[Category: Inhibitor]]
 [[Category: Serine protease]]
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