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1t9e

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[[Image:1t9e.png|left|200px]]
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==NMR solution structure of a disulfide analogue of the cyclic sunflower trypsin inhibitor SFTI-1==
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<StructureSection load='1t9e' size='340' side='right' caption='[[1t9e]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1t9e]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T9E FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sfi|1sfi]], [[1jbl|1jbl]], [[1jbn|1jbn]], [[1o8y|1o8y]], [[1o8z|1o8z]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t9e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t9e RCSB], [http://www.ebi.ac.uk/pdbsum/1t9e PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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SFTI-1 is a novel 14 amino acid peptide comprised of a circular backbone constrained by three proline residues, a hydrogen-bond network, and a single disulfide bond. It is the smallest and most potent known Bowman-Birk trypsin inhibitor and the only one with a cyclic peptidic backbone. The solution structure of [ABA(3,11)]SFTI-1, a disulfide-deficient analogue of SFTI-1, has been determined by (1)H NMR spectroscopy. The lowest energy structures of native SFTI-1 and [ABA(3,11)]SFTI-1 are similar and superimpose with a root-mean-square deviation over the backbone and heavy atoms of 0.26 +/- 0.09 and 1.10 +/- 0.22 A, respectively. The disulfide bridge in SFTI-1 was found to be a minor determinant for the overall structure, but its removal resulted in a slightly weakened hydrogen-bonding network. To further investigate the role of the disulfide bridge, NMR chemical shifts for the backbone H(alpha) protons of two disulfide-deficient linear analogues of SFTI-1, [ABA(3,11)]SFTI-1[6,5] and [ABA(3,11)]SFTI-1[1,14] were measured. These correspond to analogues of the cleavage product of SFTI-1 and a putative biosynthetic precursor, respectively. In contrast with the cyclic peptide, it was found that the disulfide bridge is essential for maintaining the structure of these open-chain analogues. Overall, the hydrogen-bond network appears to be a crucial determinant of the structure of SFTI-1 analogues.
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{{STRUCTURE_1t9e| PDB=1t9e | SCENE= }}
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Disulfide bond mutagenesis and the structure and function of the head-to-tail macrocyclic trypsin inhibitor SFTI-1.,Korsinczky ML, Clark RJ, Craik DJ Biochemistry. 2005 Feb 1;44(4):1145-53. PMID:15667208<ref>PMID:15667208</ref>
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===NMR solution structure of a disulfide analogue of the cyclic sunflower trypsin inhibitor SFTI-1===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_15667208}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1t9e]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T9E OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:015667208</ref><references group="xtra"/>
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[[Category: Clark, R J.]]
[[Category: Clark, R J.]]
[[Category: Craik, D J.]]
[[Category: Craik, D J.]]

Revision as of 06:53, 9 June 2014

NMR solution structure of a disulfide analogue of the cyclic sunflower trypsin inhibitor SFTI-1

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