1tab

<StructureSection load='1tab' size='340' side='right' caption='[[1tab]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[1tab]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TAB FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tab RCSB], [http://www.ebi.ac.uk/pdbsum/1tab PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/IBB1_PHAAN IBB1_PHAAN]] Trypsin and chymotrypsin are inhibited simultaneously. There are two separate reactive sites for trypsin and chymotrypsin but they do not inhibit simultaneously.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ta/1tab_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:3032921</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

*[[Trypsin|Trypsin]]

[[Category: Trypsin]]

[[Category: Ashida, T]]

[[Category: Ishikawa, C]]

[[Category: Kikkawa, J I]]

[[Category: Nakamura, S]]

[[Category: Takahashi, K]]

[[Category: Tanaka, I]]

[[Category: Tsunogae, Y]]

[[Category: Watanabe, K]]

[[Category: Yamane, T]]

[[Category: Serine proteinase]]