1iw4: Difference between revisions

Line 1:

[[Image:1iw4.jpg|left|200px]]<br /><applet load="1iw4" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1iw4.jpg|left|200px]]<br /><applet load="1iw4" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1iw4" />

'''Solution structure of ascidian trypsin inhibitor'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halocynthia_roretzi Halocynthia roretzi]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1IW4 OCA].

1IW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halocynthia_roretzi Halocynthia roretzi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IW4 OCA].

==Reference==

Line 30:

[[Category: trypsin inhibitor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 17~~:43:~~04 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:16 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1iw4.jpg|left|200px]]<br /><applet load="1iw4" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1iw4.jpg|left|200px]]<br /><applet load="1iw4" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1iw4" />
 '''Solution structure of ascidian trypsin inhibitor'''<br />
 ==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.
+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==
-IW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halocynthia_roretzi Halocynthia roretzi]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IW4 OCA].
+IW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halocynthia_roretzi Halocynthia roretzi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IW4 OCA].
 ==Reference==
@@ Line 30: / Line 30: @@
 [[Category: trypsin inhibitor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:43:04 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:16 2008''