1tab: Difference between revisions
New page: left|200px<br /><applet load="1tab" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tab, resolution 2.3Å" /> '''STRUCTURE OF THE TRYP... |
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[[Image:1tab.gif|left|200px]]<br /><applet load="1tab" size=" | [[Image:1tab.gif|left|200px]]<br /><applet load="1tab" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1tab, resolution 2.3Å" /> | caption="1tab, resolution 2.3Å" /> | ||
'''STRUCTURE OF THE TRYPSIN-BINDING DOMAIN OF BOWMAN-BIRK TYPE PROTEASE INHIBITOR AND ITS INTERACTION WITH TRYPSIN'''<br /> | '''STRUCTURE OF THE TRYPSIN-BINDING DOMAIN OF BOWMAN-BIRK TYPE PROTEASE INHIBITOR AND ITS INTERACTION WITH TRYPSIN'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the complex formed by bovine trypsin and | The crystal structure of the complex formed by bovine trypsin and Bowman-Birk type protease inhibitor AB-I extracted from azuki beans (Vigna angularis) 'Takara' has been analyzed. The structure was solved by the application of the phase combination of single isomorphous phases and trypsin model phases, followed by phase improvement using the iterative Fourier technique. From the resulting electron density map, a three-dimensional atomic model of the trypsin binding domain of AB-I has been built. The peptide chain at the trypsin reactive site turns back sharply at Pro29 and forms a 9-residue ring (Cys24-Cys32). The 'front side' of this ring, consisting of the reactive site (Cys24-Met28), interacts with trypsin in a similar manner to other families of inhibitors and forms a stable complex, which seems to be maintained by the interactions with the 'back side' of this ring (Pro29-Cys34). The similar spatial arrangements of the 'back side' of this inhibitor and the 'secondary contact region' of the other inhibitors with respect to the reactive site suggest an important common role of these regions in exhibiting inhibitory activity. | ||
==About this Structure== | ==About this Structure== | ||
1TAB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. 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] Full crystallographic information is available from [http:// | 1TAB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TAB OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the trypsin-binding domain of Bowman-Birk type protease inhibitor and its interaction with trypsin., Tsunogae Y, Tanaka I, Yamane T, Kikkawa J, Ashida T, Ishikawa C, Watanabe K, Nakamura S, Takahashi K, J Biochem | Structure of the trypsin-binding domain of Bowman-Birk type protease inhibitor and its interaction with trypsin., Tsunogae Y, Tanaka I, Yamane T, Kikkawa J, Ashida T, Ishikawa C, Watanabe K, Nakamura S, Takahashi K, J Biochem. 1986 Dec;100(6):1637-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3032921 3032921] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
[[Category: Ashida, T.]] | [[Category: Ashida, T.]] | ||
[[Category: Ishikawa, C.]] | [[Category: Ishikawa, C.]] | ||
[[Category: Kikkawa, J | [[Category: Kikkawa, J I.]] | ||
[[Category: Nakamura, S.]] | [[Category: Nakamura, S.]] | ||
[[Category: Takahashi, K.]] | [[Category: Takahashi, K.]] | ||
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[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:36 2008'' | ||
Revision as of 16:11, 21 February 2008
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STRUCTURE OF THE TRYPSIN-BINDING DOMAIN OF BOWMAN-BIRK TYPE PROTEASE INHIBITOR AND ITS INTERACTION WITH TRYPSIN
OverviewOverview
The crystal structure of the complex formed by bovine trypsin and Bowman-Birk type protease inhibitor AB-I extracted from azuki beans (Vigna angularis) 'Takara' has been analyzed. The structure was solved by the application of the phase combination of single isomorphous phases and trypsin model phases, followed by phase improvement using the iterative Fourier technique. From the resulting electron density map, a three-dimensional atomic model of the trypsin binding domain of AB-I has been built. The peptide chain at the trypsin reactive site turns back sharply at Pro29 and forms a 9-residue ring (Cys24-Cys32). The 'front side' of this ring, consisting of the reactive site (Cys24-Met28), interacts with trypsin in a similar manner to other families of inhibitors and forms a stable complex, which seems to be maintained by the interactions with the 'back side' of this ring (Pro29-Cys34). The similar spatial arrangements of the 'back side' of this inhibitor and the 'secondary contact region' of the other inhibitors with respect to the reactive site suggest an important common role of these regions in exhibiting inhibitory activity.
About this StructureAbout this Structure
1TAB is a Protein complex structure of sequences from [1]. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
ReferenceReference
Structure of the trypsin-binding domain of Bowman-Birk type protease inhibitor and its interaction with trypsin., Tsunogae Y, Tanaka I, Yamane T, Kikkawa J, Ashida T, Ishikawa C, Watanabe K, Nakamura S, Takahashi K, J Biochem. 1986 Dec;100(6):1637-46. PMID:3032921
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