1ldt: Difference between revisions
New page: left|200px<br /> <applet load="1ldt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ldt, resolution 1.9Å" /> '''COMPLEX OF LEECH-DER... |
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[[Image:1ldt.gif|left|200px]]<br /> | [[Image:1ldt.gif|left|200px]]<br /><applet load="1ldt" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1ldt" size=" | |||
caption="1ldt, resolution 1.9Å" /> | caption="1ldt, resolution 1.9Å" /> | ||
'''COMPLEX OF LEECH-DERIVED TRYPTASE INHIBITOR WITH PORCINE TRYPSIN'''<br /> | '''COMPLEX OF LEECH-DERIVED TRYPTASE INHIBITOR WITH PORCINE TRYPSIN'''<br /> | ||
==Overview== | ==Overview== | ||
The x-ray crystal structure of recombinant leech-derived tryptase | The x-ray crystal structure of recombinant leech-derived tryptase inhibitor (rLDTI) has been solved to a resolution of 1.9 A in complex with porcine trypsin. The nonclassical Kazal-type inhibitor exhibits the same overall architecture as that observed in solution and in rhodniin. The complex reveals structural aspects of the mast cell proteinase tryptase. The conformation of the binding region of rLDTI suggests that tryptase has a restricted active site cleft. The basic amino terminus of rLDTI, apparently flexible from previous NMR measurements, approaches the 148-loop of trypsin. This loop has an acidic equivalent in tryptase, suggesting that the basic amino terminus could make favorable electrostatic interactions with the tryptase molecule. A series of rLDTI variants constructed to probe this hypothesis confirmed that the amino-terminal Lys-Lys sequence plays a role in inhibition of human lung tryptase but not of trypsin or chymotrypsin. The location of such an acidic surface patch is in accordance with the known low molecular weight inhibitors of tryptase. | ||
==About this Structure== | ==About this Structure== | ||
1LDT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http:// | 1LDT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LDT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
[[Category: Stubbs, M | [[Category: Stubbs, M T.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: complex (hydrolase/inhibitor)]] | [[Category: complex (hydrolase/inhibitor)]] | ||
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[[Category: tryptase]] | [[Category: tryptase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:03 2008'' | ||
Revision as of 14:44, 21 February 2008
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COMPLEX OF LEECH-DERIVED TRYPTASE INHIBITOR WITH PORCINE TRYPSIN
OverviewOverview
The x-ray crystal structure of recombinant leech-derived tryptase inhibitor (rLDTI) has been solved to a resolution of 1.9 A in complex with porcine trypsin. The nonclassical Kazal-type inhibitor exhibits the same overall architecture as that observed in solution and in rhodniin. The complex reveals structural aspects of the mast cell proteinase tryptase. The conformation of the binding region of rLDTI suggests that tryptase has a restricted active site cleft. The basic amino terminus of rLDTI, apparently flexible from previous NMR measurements, approaches the 148-loop of trypsin. This loop has an acidic equivalent in tryptase, suggesting that the basic amino terminus could make favorable electrostatic interactions with the tryptase molecule. A series of rLDTI variants constructed to probe this hypothesis confirmed that the amino-terminal Lys-Lys sequence plays a role in inhibition of human lung tryptase but not of trypsin or chymotrypsin. The location of such an acidic surface patch is in accordance with the known low molecular weight inhibitors of tryptase.
About this StructureAbout this Structure
1LDT is a Protein complex structure of sequences from Hirudo medicinalis and Sus scrofa with as ligand. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition., Stubbs MT, Morenweiser R, Sturzebecher J, Bauer M, Bode W, Huber R, Piechottka GP, Matschiner G, Sommerhoff CP, Fritz H, Auerswald EA, J Biol Chem. 1997 Aug 8;272(32):19931-7. PMID:9242660
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