1an1
From Proteopedia
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(New page: 200px<br /> <applet load="1an1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1an1, resolution 2.03Å" /> '''LEECH-DERIVED TRYPT...)
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Revision as of 14:57, 29 October 2007
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LEECH-DERIVED TRYPTASE INHIBITOR/TRYPSIN COMPLEX
Overview
BACKGROUND: Tryptase is a trypsin-like serine proteinase stored in the, cytoplasmic granules of mast cells, which has been implicated in a number, of mast cell related disorders such as asthma and rheumatoid arthritis., Unlike almost all other serine proteinases, tryptase is fully active in, plasma and in the extracellular space, as there are no known natural, inhibitors of tryptase in humans. Leech-derived tryptase inhibitor (LDTI), a protein of 46 amino acids, is the first molecule found to bind tightly, to and specifically inhibit human tryptase in the nanomolar range. LDTI, also inhibits trypsin and chymotrypsin with similar affinities. The, structure of LDTI in complex with an inhibited proteinase could be used as, a template for the development of low molecular weight tryptase, ... [(full description)]
About this Structure
1AN1 is a [Protein complex] structure of sequences from [Hirudo medicinalis] and [Sus scrofa] with CA as [ligand]. Active as [[1]], with EC number [3.4.21.4]. Full crystallographic information is available from [OCA].
Reference
Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LDTI-tryptase system., Di Marco S, Priestle JP, Structure. 1997 Nov 15;5(11):1465-74. PMID:9384562
Page seeded by OCA on Mon Oct 29 17:01:42 2007
