| pubmed-article:12621047 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12621047 | lifeskim:mentions | umls-concept:C0010546 | lld:lifeskim |
| pubmed-article:12621047 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:12621047 | lifeskim:mentions | umls-concept:C0033607 | lld:lifeskim |
| pubmed-article:12621047 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:12621047 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12621047 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:12621047 | lifeskim:mentions | umls-concept:C1709634 | lld:lifeskim |
| pubmed-article:12621047 | lifeskim:mentions | umls-concept:C1571575 | lld:lifeskim |
| pubmed-article:12621047 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:12621047 | pubmed:dateCreated | 2003-6-9 | lld:pubmed |
| pubmed-article:12621047 | pubmed:abstractText | The most potent known naturally occurring Bowman-Birk inhibitor, sunflower trypsin inhibitor-1 (SFTI-1), is a bicyclic 14-amino acid peptide from sunflower seeds comprising one disulfide bond and a cyclic backbone. At present, little is known about the cyclization mechanism of SFTI-1. We show here that an acyclic permutant of SFTI-1 open at its scissile bond, SFTI-1[6,5], also functions as an inhibitor of trypsin and that it can be enzymatically backbone-cyclized by incubation with bovine beta-trypsin. The resulting ratio of cyclic SFTI-1 to SFTI-1[6,5] is approximately 9:1 regardless of whether trypsin is incubated with SFTI-1[6,5] or SFTI-1. Enzymatic resynthesis of the scissile bond to form cyclic SFTI-1 is a novel mechanism of cyclization of SFTI-1[6,5]. Such a reaction could potentially occur on a trypsin affinity column as used in the original isolation procedure of SFTI-1. We therefore extracted SFTI-1 from sunflower seeds without a trypsin purification step and confirmed that the backbone of SFTI-1 is indeed naturally cyclic. Structural studies on SFTI-1[6,5] revealed high heterogeneity, and multiple species of SFTI-1[6,5] were identified. The main species closely resembles the structure of cyclic SFTI-1 with the broken binding loop able to rotate between a cis/trans geometry of the I7-P8 bond with the cis conformer being similar to the canonical binding loop conformation. The non-reactive loop adopts a beta-hairpin structure as in cyclic wild-type SFTI-1. Another species exhibits an iso-aspartate residue at position 14 and provides implications for possible in vivo cyclization mechanisms. | lld:pubmed |
| pubmed-article:12621047 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12621047 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12621047 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12621047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12621047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12621047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12621047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12621047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12621047 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12621047 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12621047 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12621047 | pubmed:author | pubmed-author:JonesAlunA | lld:pubmed |
| pubmed-article:12621047 | pubmed:author | pubmed-author:CraikDavid... | lld:pubmed |
| pubmed-article:12621047 | pubmed:author | pubmed-author:OtvosLaszloLJ... | lld:pubmed |
| pubmed-article:12621047 | pubmed:author | pubmed-author:MarxUte CUC | lld:pubmed |
| pubmed-article:12621047 | pubmed:author | pubmed-author:SchirraHorst... | lld:pubmed |
| pubmed-article:12621047 | pubmed:author | pubmed-author:KorsinczkyMic... | lld:pubmed |
| pubmed-article:12621047 | pubmed:author | pubmed-author:CondieBarrieB | lld:pubmed |
| pubmed-article:12621047 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12621047 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:12621047 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12621047 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12621047 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12621047 | pubmed:pagination | 21782-9 | lld:pubmed |
| pubmed-article:12621047 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:12621047 | pubmed:meshHeading | pubmed-meshheading:12621047... | lld:pubmed |
| pubmed-article:12621047 | pubmed:meshHeading | pubmed-meshheading:12621047... | lld:pubmed |
| pubmed-article:12621047 | pubmed:meshHeading | pubmed-meshheading:12621047... | lld:pubmed |
| pubmed-article:12621047 | pubmed:meshHeading | pubmed-meshheading:12621047... | lld:pubmed |
| pubmed-article:12621047 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12621047 | pubmed:articleTitle | Enzymatic cyclization of a potent bowman-birk protease inhibitor, sunflower trypsin inhibitor-1, and solution structure of an acyclic precursor peptide. | lld:pubmed |
| pubmed-article:12621047 | pubmed:affiliation | Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia. | lld:pubmed |
| pubmed-article:12621047 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12621047 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12621047 | lld:pubmed |
