1bip

<StructureSection load='1bip' size='340' side='right'caption='[[1bip]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

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

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bip OCA], [https://pdbe.org/1bip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bip RCSB], [https://www.ebi.ac.uk/pdbsum/1bip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bip ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/IAAT_ELECO IAAT_ELECO]] May play a protective role against endo- and exogenous hydrolytic activities in the Ragi seeds.

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== Publication Abstract from PubMed ==

The three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor (RBI) from seeds of ragi (Eleusine coracana Gaertneri) has been determined in solution using multidimensional 1H and 15N NMR spectroscopy. The inhibitor consists of 122 amino acids, with 5 disulfide bridges, and belongs to the plant alpha-amylase/trypsin inhibitor family for which no three-dimensional structures have yet been available. The structure of the inhibitor was determined on the basis of 1131 interresidue interproton distance constraints derived from nuclear Overhauser enhancement measurements and 52 phi angles, supplemented by 9 psi and 51 chi 1 angles. RBI consists of a globular four-helix motif with a simple "up-and-down" topology. The helices are between residues 18-29, 37-51, 58-65, and 87-94. A fragment from Val 67 to Ser 69 and Gln 73 to Glu 75 forms an antiparallel beta-sheet. The fold of RBI represents a new motif among the serine proteinase inhibitors. The trypsin binding loop of RBI adopts the "canonical", substrate-like conformation which is highly conserved among serine proteinase inhibitors. The binding loop is stabilized by the two adjacent alpha-helices 1 and 2. This motif is also novel and not found in known structures of serine proteinase inhibitors. The three-dimensional structure of RBI together with biochemical data suggests the location of the alpha-amylase binding site on the face of the molecule opposite to the site of the trypsin binding loop. The RBI fold should be general for all members of the RBI family because conserved residues among the members of the family from the core of the structure.

Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy.,Strobl S, Muhlhahn P, Bernstein R, Wiltscheck R, Maskos K, Wunderlich M, Huber R, Glockshuber R, Holak TA Biochemistry. 1995 Jul 4;34(26):8281-93. PMID:7599120<ref>PMID:7599120</ref>

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

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<div class="pdbe-citations 1bip" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Eleco]]

[[Category: Holak, T]]

[[Category: Muehlhahn, P]]

[[Category: Strobl, S]]

[[Category: Serine proteinase inhibitor]]