02062nas a2200205   4500008004100000022001400041245011100055210006900166260007300235300001400308490000900322520124800331653003501579653002901614653003201643653002201675100001601697700001901713856012401732       2007                        eng d  a1570-963900aBowman-birk protease inhibitor from the seeds of vigna unguiculata forms a highly stable dimeric structure0 aBowmanbirk protease inhibitor from the seeds of vigna unguiculat  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcOCT  a1264-12730 v17743 a<p>Different protease inhibitors including Bowman-Birk type (BBI) have been reported from the seeds of rigna unguiculata. Protease isoinhibitors of double-headed Bowman-Birk type from the seeds of Vigna unguiculata have been purified and characterized. The BBI from Vigna unguiculata (Vu-BBI) has been found to undergo self-association to form very stable dimers and more complex oligomers, by size-exclusion chromatography and SDS-PAGE in the presence of urea. Many BBIs have been reported to undergo self-association to form homodimers or more complex oligomers in solution. Only one dimeric crystal structure of a BBI (pea-BBI) is reported to date. We report the three-dimensional structure of a Vu-BBI determined at 2.5 A resolution. Although, the inhibitor has a monomer fold similar to that found in other known structures of Bowman-Birk protease inhibitors, its quaternary structure is different from that commonly observed in this family. The structural elements responsible for the stability of monomer molecule and dimeric association are discussed. The Vu-BBI may use dimeric or higher quaternary association to maintain the physiological state and to execute its biological function. (C) 2007 Elsevier B.V. All rights reserved.</p>10aBowman-Birk protease inhibitor10aplant protease inhibitor10aprotein-protein interaction10aVigna unguiculata1 aRao, K., N.1 aSuresh, C., G.  uhttps://library.ncl.res.in/content/bowman-birk-protease-inhibitor-seeds-vigna-unguiculata-forms-highly-stable-dimeric-0