1t9e
From Proteopedia
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|PDB= 1t9e |SIZE=350|CAPTION= <scene name='initialview01'>1t9e</scene> | |PDB= 1t9e |SIZE=350|CAPTION= <scene name='initialview01'>1t9e</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1sfi|1SFI]], [[1jbl|1JBL]], [[1jbn|1JBN]], [[1o8y|1O8Y]], [[1o8z|1O8Z]] | ||
| + | |RESOURCES=<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.ebi.ac.uk/pdbsum/1t9e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t9e RCSB]</span> | ||
}} | }} | ||
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[[Category: sunflower trypsin inhibitor]] | [[Category: sunflower trypsin inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:53:12 2008'' |
Revision as of 20:53, 30 March 2008
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| Ligands: | |||||||
| Related: | 1SFI, 1JBL, 1JBN, 1O8Y, 1O8Z
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR solution structure of a disulfide analogue of the cyclic sunflower trypsin inhibitor SFTI-1
Overview
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.
About this Structure
1T9E is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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
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