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| - | [[Image:2f9p.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2f9p| PDB=2f9p | SCENE= }} | | {{STRUCTURE_2f9p| PDB=2f9p | SCENE= }} |
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| - | '''Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G in Complex with Leupeptin'''
| + | ===Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G in Complex with Leupeptin=== |
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| - | ==Overview==
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| - | Tryptases alpha and beta are trypsin-like serine proteinases expressed in large amounts by mast cells. Beta-tryptase is a tetramer that has enzymatic activity, but requires heparin binding to maintain functional and structural stability, whereas alpha-tryptase has little, if any, enzymatic activity but is a stable tetramer in the absence of heparin. As shown previously, these differences can be mainly attributed to the different conformations of the 214-220 segment. Interestingly, the replacement of Asp216 by Gly, which is present in beta-tryptase, results in enzymatically active but less stable alpha-tryptase mutants. We have solved the crystal structures of both the single (D216G) and the double (K192Q/D216G) mutant forms of recombinant human alphaI-tryptase in complex with the peptide inhibitor leupeptin, as well as the structure of the non-inhibited single mutant. The inhibited mutants exhibited an open functional substrate binding site, while in the absence of an inhibitor, the open (beta-tryptase-like) and the closed (alpha-tryptase-like) conformations were present simultaneously. This shows that both forms are in a two-state equilibrium, which is influenced by the residues in the vicinity of the active site and by inhibitor/substrate binding. Novel insights regarding the observed stability differences as well as a potential proteolytic activity of wild-type alpha-tryptase, which may possess a cryptic active site, are discussed.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16414069}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16414069 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16414069}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Serine proteinase]] | | [[Category: Serine proteinase]] |
| | [[Category: Trypsin-like]] | | [[Category: Trypsin-like]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:38:13 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:59:51 2008'' |
Revision as of 20:59, 27 July 2008
Template:STRUCTURE 2f9p
Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G in Complex with Leupeptin
Template:ABSTRACT PUBMED 16414069
About this Structure
2F9P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha-->beta-tryptase transition., Rohr KB, Selwood T, Marquardt U, Huber R, Schechter NM, Bode W, Than ME, J Mol Biol. 2006 Mar 17;357(1):195-209. Epub 2005 Dec 28. PMID:16414069
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