1a0l
From Proteopedia
(New page: 200px<br /> <applet load="1a0l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a0l, resolution 3.0Å" /> '''HUMAN BETA-TRYPTASE:...) |
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| - | [[Image:1a0l.gif|left|200px]]<br /> | + | [[Image:1a0l.gif|left|200px]]<br /><applet load="1a0l" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1a0l" size=" | + | |
caption="1a0l, resolution 3.0Å" /> | caption="1a0l, resolution 3.0Å" /> | ||
'''HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE'''<br /> | '''HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human tryptase, a mast-cell-specific serine proteinase that may be | + | Human tryptase, a mast-cell-specific serine proteinase that may be involved in causing asthma and other allergic and inflammatory disorders, is unique in two respects: it is enzymatically active only as a heparin-stabilized tetramer, and it is resistant to all known endogenous proteinase inhibitors. The 3-A crystal structure of human beta-tryptase in a complex with 4-amidinophenyl pyruvic acid shows four quasi-equivalent monomers arranged in a square flat ring of pseudo 222 symmetry. Each monomer contacts its neighbours at two different interfaces through six loop segments. These loops are located around the active site of beta-tryptase and differ considerably in length and conformation from loops of other trypsin-like proteinases. The four active centres of the tetramer are directed towards an oval central pore, restricting access for macromolecular substrates and enzyme inhibitors. Heparin chains might stabilize the complex by binding to an elongated patch of positively charged residues spanning two adjacent monomers. The nature of this unique tetrameric architecture explains many of tryptase's biochemical properties and provides a basis for the rational design of monofunctional and bifunctional tryptase inhibitors. |
==About this Structure== | ==About this Structure== | ||
| - | 1A0L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with APA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tryptase Tryptase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.59 3.4.21.59] Full crystallographic information is available from [http:// | + | 1A0L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=APA:'>APA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tryptase Tryptase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.59 3.4.21.59] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Macedo-Ribeiro, S.]] | [[Category: Macedo-Ribeiro, S.]] | ||
[[Category: Matschiner, G.]] | [[Category: Matschiner, G.]] | ||
| - | [[Category: Pereira, P | + | [[Category: Pereira, P J.B.]] |
| - | [[Category: Sommerhoff, C | + | [[Category: Sommerhoff, C P.]] |
[[Category: APA]] | [[Category: APA]] | ||
[[Category: allergy]] | [[Category: allergy]] | ||
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[[Category: trypsin-like serine proteinase]] | [[Category: trypsin-like serine proteinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:31 2008'' |
Revision as of 09:39, 21 February 2008
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HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE
Overview
Human tryptase, a mast-cell-specific serine proteinase that may be involved in causing asthma and other allergic and inflammatory disorders, is unique in two respects: it is enzymatically active only as a heparin-stabilized tetramer, and it is resistant to all known endogenous proteinase inhibitors. The 3-A crystal structure of human beta-tryptase in a complex with 4-amidinophenyl pyruvic acid shows four quasi-equivalent monomers arranged in a square flat ring of pseudo 222 symmetry. Each monomer contacts its neighbours at two different interfaces through six loop segments. These loops are located around the active site of beta-tryptase and differ considerably in length and conformation from loops of other trypsin-like proteinases. The four active centres of the tetramer are directed towards an oval central pore, restricting access for macromolecular substrates and enzyme inhibitors. Heparin chains might stabilize the complex by binding to an elongated patch of positively charged residues spanning two adjacent monomers. The nature of this unique tetrameric architecture explains many of tryptase's biochemical properties and provides a basis for the rational design of monofunctional and bifunctional tryptase inhibitors.
About this Structure
1A0L is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Tryptase, with EC number 3.4.21.59 Full crystallographic information is available from OCA.
Reference
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore., Pereira PJ, Bergner A, Macedo-Ribeiro S, Huber R, Matschiner G, Fritz H, Sommerhoff CP, Bode W, Nature. 1998 Mar 19;392(6673):306-11. PMID:9521329
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