1a0l

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{{Seed}}
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{{STRUCTURE_1a0l| PDB=1a0l | SCENE= }}
{{STRUCTURE_1a0l| PDB=1a0l | SCENE= }}
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'''HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE'''
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===HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_9521329}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 9521329 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9521329}}
==About this Structure==
==About this Structure==
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[[Category: Tetramer]]
[[Category: Tetramer]]
[[Category: Trypsin-like serine proteinase]]
[[Category: Trypsin-like serine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:37:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:44:14 2008''

Revision as of 12:44, 30 June 2008

Image:1a0l.png

Template:STRUCTURE 1a0l

HUMAN BETA-TRYPTASE: A RING-LIKE TETRAMER WITH ACTIVE SITES FACING A CENTRAL PORE

Template:ABSTRACT PUBMED 9521329

About this Structure

1A0L is a Single protein structure of sequence from Homo sapiens. 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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