1iw4
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iw4 OCA], [http://www.ebi.ac.uk/pdbsum/1iw4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iw4 RCSB]</span> | ||
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[[Category: trypsin inhibitor]] | [[Category: 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 21:25:38 2008'' |
Revision as of 18:25, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of ascidian trypsin inhibitor
Overview
The three-dimensional solution structure of ascidian trypsin inhibitor (ATI), a 55 amino acid residue protein with four disulfide bridges, was determined by means of two-dimensional nuclear magnetic resonance (2D NMR) spectroscopy. The resulting structure of ATI was characterized by an alpha-helical conformation in residues 35-42 and a three-stranded antiparallel beta-sheet in residues 22-26, 29-32, and 48-50. The presence of an alpha-helical conformation was predicted from the consensus sequences of the cystine-stabilized alpha-helical (CSH) motif, which is characterized by an alpha-helix structure in the Cys-X(1)-X(2)-X(3)-Cys portion (corresponding to residues 37-41), linking to the Cys-X-Cys portion (corresponding to residues 12-14) folded in an extended structure. The secondary structure and the overall folding of the main chain of ATI were very similar to those of the Kazal-type inhibitors, such as Japanese quail ovomucoid third domain (OMJPQ3) and leech-derived tryptase inhibitor form C (LDTI-C), although ATI does not show extensive sequence homology to these inhibitors except for a few amino acid residues and six of eight half-cystines. On the basis of these findings, we realign the amino acid sequences of representative Kazal-type inhibitors including ATI and discuss the unique structure of ATI with four disulfide bridges.
About this Structure
1IW4 is a Single protein structure of sequence from Halocynthia roretzi. Full crystallographic information is available from OCA.
Reference
Solution structure of ascidian trypsin inhibitor determined by nuclear magnetic resonance spectroscopy., Hemmi H, Yoshida T, Kumazaki T, Nemoto N, Hasegawa J, Nishioka F, Kyogoku Y, Yokosawa H, Kobayashi Y, Biochemistry. 2002 Aug 27;41(34):10657-64. PMID:12186551
Page seeded by OCA on Sun Mar 30 21:25:38 2008
Categories: Halocynthia roretzi | Single protein | Hasegawa, J. | Hemmi, H. | Kobayashi, Y. | Kumazaki, T. | Kyogoku, Y. | Nemoto, N. | Nishioka, F. | Yokosawa, H. | Yoshida, T. | Ascidian | Cystine-stabilized alpha-helical motif | Disulfide bond | Kazal-type inhibitor | Nmr | Solution structure | Trypsin inhibitor
