1ldt: Difference between revisions
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[[Image:1ldt.gif|left|200px]] | [[Image:1ldt.gif|left|200px]] | ||
'''COMPLEX OF LEECH-DERIVED TRYPTASE INHIBITOR WITH PORCINE TRYPSIN''' | {{Structure | ||
|PDB= 1ldt |SIZE=350|CAPTION= <scene name='initialview01'>1ldt</scene>, resolution 1.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''COMPLEX OF LEECH-DERIVED TRYPTASE INHIBITOR WITH PORCINE TRYPSIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LDT is a [ | 1LDT is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LDT OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9242660 9242660] | ||
[[Category: Hirudo medicinalis]] | [[Category: Hirudo medicinalis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: tryptase]] | [[Category: tryptase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:29:46 2008'' | ||
Revision as of 13:29, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | |||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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