1avu
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1avu.gif|left|200px]]<br /><applet load="1avu" size=" | + | [[Image:1avu.gif|left|200px]]<br /><applet load="1avu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1avu, resolution 2.30Å" /> | caption="1avu, resolution 2.30Å" /> | ||
'''TRYPSIN INHIBITOR FROM SOYBEAN (STI)'''<br /> | '''TRYPSIN INHIBITOR FROM SOYBEAN (STI)'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1AVU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Known structural/functional Site: <scene name='pdbsite=ACT:P1 Site'>ACT</scene>. Full crystallographic information is available from [http:// | + | 1AVU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Known structural/functional Site: <scene name='pdbsite=ACT:P1+Site'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVU OCA]. |
==Reference== | ==Reference== | ||
| Line 20: | Line 20: | ||
[[Category: trypsin inhibitor]] | [[Category: trypsin inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:31:47 2008'' |
Revision as of 07:31, 3 February 2008
|
TRYPSIN INHIBITOR FROM SOYBEAN (STI)
Overview
The Kunitz-type trypsin inhibitor from soybean (STI) consists of 181 amino, acid residues with two disulfide bridges. Its crystal structures have been, determined in complex with porcine pancreatic trypsin in two crystal forms, (an orthorhombic form at 1.75 A resolution and a tetragonal form at 1.9 A), and in the free state at 2.3 A resolution. They have been refined to, crystallographic R-values of 18.9%, 21.6% and 19.8%, respectively. The, three models of STI reported here represent a significant improvement over, the partial inhibitor structure in the complex, which was previously, determined at a nominal resolution of 2.6 A by the multiple isomorphous, replacement method. This study provides the first high-resolution picture, of the complex between a Kunitz-type proteinase inhibitor with its cognate, proteinase. Many of the external loops of STI show high B-factors, both in, the free and the complexed states, except the reactive site loop whose, B-factors are dramatically reduced upon complexation. The reactive site, loop of STI adopts a canonical conformation similar to those in other, substrate-like inhibitors. The P1 carbonyl group displays no out-of-plane, displacement and thus retains a nominal trigonal planar geometry. Modeling, studies on the complex between a homologous Kunitz-type trypsin inhibitor, DE-3 from Erythrina caffra and the human tissue-type plasminogen activator, reveal a new insight into the specific interactions which could play a, crucial role in their binding.
About this Structure
1AVU is a Single protein structure of sequence from Glycine max. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator., Song HK, Suh SW, J Mol Biol. 1998 Jan 16;275(2):347-63. PMID:9466914
Page seeded by OCA on Sun Feb 3 09:31:47 2008
