1tps
From Proteopedia
(New page: 200px<br /><applet load="1tps" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tps, resolution 1.9Å" /> '''ATOMIC STRUCTURE OF T...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1tps.jpg|left|200px]]<br /><applet load="1tps" size=" | + | [[Image:1tps.jpg|left|200px]]<br /><applet load="1tps" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tps, resolution 1.9Å" /> | caption="1tps, resolution 1.9Å" /> | ||
'''ATOMIC STRUCTURE OF THE TRYPSIN-A90720A COMPLEX: A UNIFIED APPROACH TO STRUCTURE AND FUNCTION'''<br /> | '''ATOMIC STRUCTURE OF THE TRYPSIN-A90720A COMPLEX: A UNIFIED APPROACH TO STRUCTURE AND FUNCTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: A90720A is a potent serine proteinase inhibitor produced by | + | BACKGROUND: A90720A is a potent serine proteinase inhibitor produced by the terrestrial blue-green alga Microchaete loktakensis. Most of its structure has been defined by spectroscopic and degradative studies, but the configurations of several stereochemical centers are unknown, and its mode of inhibition of serine proteinases is not understood. We therefore examined the structure of the compound in a complex with trypsin. RESULTS: We have crystallized the bovine trypsin-A90720A complex and determined its three-dimensional structure at 1.90 A resolution using single crystal X-ray diffraction. The structure of the bound inhibitor is clearly shown in the electron density. The structure defines the absolute stereostructure of A90720A, establishes its bound conformation and illuminates its mode of inhibition. CONCLUSIONS: A90720A interacts with trypsin in a substrate-like manner through an extensive series of hydrogen bonds, hydrophobic interactions and steric complementarity. The compound uses a mixture of peptidal and nonpeptidal elements to imitate the canonical conformation of the exposed binding loop of 'small' proteinase inhibitors. |
==About this Structure== | ==About this Structure== | ||
| - | 1TPS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA and A9A as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1TPS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=A9A:'>A9A</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPS OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Clardy, J.]] | [[Category: Clardy, J.]] | ||
| - | [[Category: Lee, A | + | [[Category: Lee, A Y.]] |
[[Category: A9A]] | [[Category: A9A]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: hydrolase(serine protease)]] | [[Category: hydrolase(serine protease)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:07 2008'' |
Revision as of 13:16, 21 February 2008
|
ATOMIC STRUCTURE OF THE TRYPSIN-A90720A COMPLEX: A UNIFIED APPROACH TO STRUCTURE AND FUNCTION
Overview
BACKGROUND: A90720A is a potent serine proteinase inhibitor produced by the terrestrial blue-green alga Microchaete loktakensis. Most of its structure has been defined by spectroscopic and degradative studies, but the configurations of several stereochemical centers are unknown, and its mode of inhibition of serine proteinases is not understood. We therefore examined the structure of the compound in a complex with trypsin. RESULTS: We have crystallized the bovine trypsin-A90720A complex and determined its three-dimensional structure at 1.90 A resolution using single crystal X-ray diffraction. The structure of the bound inhibitor is clearly shown in the electron density. The structure defines the absolute stereostructure of A90720A, establishes its bound conformation and illuminates its mode of inhibition. CONCLUSIONS: A90720A interacts with trypsin in a substrate-like manner through an extensive series of hydrogen bonds, hydrophobic interactions and steric complementarity. The compound uses a mixture of peptidal and nonpeptidal elements to imitate the canonical conformation of the exposed binding loop of 'small' proteinase inhibitors.
About this Structure
1TPS is a Single protein structure of sequence from Bos taurus with and as ligands. Full crystallographic information is available from OCA.
Reference
Atomic structure of the trypsin-A90720A complex: a unified approach to structure and function., Lee AY, Smitka TA, Bonjouklian R, Clardy J, Chem Biol. 1994 Oct;1(2):113-7. PMID:9383379
Page seeded by OCA on Thu Feb 21 15:16:07 2008
