1avw: Difference between revisions

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[[Image:1avw.gif|left|200px]]<br /><applet load="1avw" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1avw.gif|left|200px]]
caption="1avw, resolution 1.75&Aring;" />
 
'''COMPLEX PORCINE PANCREATIC TRYPSIN/SOYBEAN TRYPSIN INHIBITOR, ORTHORHOMBIC CRYSTAL FORM'''<br />
{{Structure
|PDB= 1avw |SIZE=350|CAPTION= <scene name='initialview01'>1avw</scene>, resolution 1.75&Aring;
|SITE= <scene name='pdbsite=AVE:Catalytic+Triad'>AVE</scene> and <scene name='pdbsite=IRY:P1+Site'>IRY</scene>
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4]
|GENE=
}}
 
'''COMPLEX PORCINE PANCREATIC TRYPSIN/SOYBEAN TRYPSIN INHIBITOR, ORTHORHOMBIC CRYSTAL FORM'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1AVW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Glycine_max Glycine max] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Known structural/functional Sites: <scene name='pdbsite=AVE:Catalytic+Triad'>AVE</scene> and <scene name='pdbsite=IRY:P1+Site'>IRY</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVW OCA].  
1AVW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Glycine_max Glycine max] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVW OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9466914 9466914]
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:[http://www.ncbi.nlm.nih.gov/pubmed/9466914 9466914]
[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: soybean trypsin inhibitor]]
[[Category: soybean trypsin inhibitor]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:47 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:55 2008''

Revision as of 11:02, 20 March 2008

File:1avw.gif


PDB ID 1avw

Drag the structure with the mouse to rotate
, resolution 1.75Å
Sites: and
Ligands:
Activity: Trypsin, with EC number 3.4.21.4
Coordinates: save as pdb, mmCIF, xml



COMPLEX PORCINE PANCREATIC TRYPSIN/SOYBEAN TRYPSIN INHIBITOR, ORTHORHOMBIC CRYSTAL FORM


OverviewOverview

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 StructureAbout this Structure

1AVW is a Protein complex structure of sequences from Glycine max and Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

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

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