1r02: Difference between revisions

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[[Image:1r02.gif|left|200px]]<br />

[[Image:1r02.gif|left|200px]]<br /><applet load="1r02" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1r02" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1r02" />

'''Solution structure of Human Orexin-A:Regulator of Appetite and Wakefulness'''<br />

==Overview==

Orexin-A and orexin-B (hypocretin-1 and hypocretin-2, respectively) are, important hypothalamic neuro-peptides, which are encoded by a single mRNA, transcript and stimulate food intake as well as regulate wakefulness. Here, we determined the solution structure of orexin-A by NMR spectroscopy and, by simulated-annealing calculation. The structural features of orexin-A, involve two alpha-helices, with the hydrophobic residues disposed to on, one side of helix, and hydrophilic residues to the other. A hydrophilic, turn induced by two disulfide bonds provides the key difference between, orexin-A and -B. With previous mutagenic studies, the derived structure of, orexin-A provides us with a structure-functional view for novel drug, design.

Orexin-A and orexin-B (hypocretin-1 and hypocretin-2, respectively) are important hypothalamic neuro-peptides, which are encoded by a single mRNA transcript and stimulate food intake as well as regulate wakefulness. Here we determined the solution structure of orexin-A by NMR spectroscopy and by simulated-annealing calculation. The structural features of orexin-A involve two alpha-helices, with the hydrophobic residues disposed to on one side of helix, and hydrophilic residues to the other. A hydrophilic turn induced by two disulfide bonds provides the key difference between orexin-A and -B. With previous mutagenic studies, the derived structure of orexin-A provides us with a structure-functional view for novel drug design.

==Disease==

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==About this Structure==

1R02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1R02 OCA].

1R02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R02 OCA].

==Reference==

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[[Category: Single protein]]

[[Category: Hong, E.]]

[[Category: Kim, H.Y.]]

[[Category: Kim, H Y.]]

[[Category: Kim, J.I.]]

[[Category: Kim, J I.]]

[[Category: Lee, W.]]

[[Category: helix-loop-helix]]

[[Category: turn]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 18~~:58:~~02 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:31 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1r02.gif|left|200px]]<br />
+[[Image:1r02.gif|left|200px]]<br /><applet load="1r02" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1r02" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1r02" />
 '''Solution structure of Human Orexin-A:Regulator of Appetite and Wakefulness'''<br />
 ==Overview==
-Orexin-A and orexin-B (hypocretin-1 and hypocretin-2, respectively) are, important hypothalamic neuro-peptides, which are encoded by a single mRNA, transcript and stimulate food intake as well as regulate wakefulness. Here, we determined the solution structure of orexin-A by NMR spectroscopy and, by simulated-annealing calculation. The structural features of orexin-A, involve two alpha-helices, with the hydrophobic residues disposed to on, one side of helix, and hydrophilic residues to the other. A hydrophilic, turn induced by two disulfide bonds provides the key difference between, orexin-A and -B. With previous mutagenic studies, the derived structure of, orexin-A provides us with a structure-functional view for novel drug, design.
+Orexin-A and orexin-B (hypocretin-1 and hypocretin-2, respectively) are important hypothalamic neuro-peptides, which are encoded by a single mRNA transcript and stimulate food intake as well as regulate wakefulness. Here we determined the solution structure of orexin-A by NMR spectroscopy and by simulated-annealing calculation. The structural features of orexin-A involve two alpha-helices, with the hydrophobic residues disposed to on one side of helix, and hydrophilic residues to the other. A hydrophilic turn induced by two disulfide bonds provides the key difference between orexin-A and -B. With previous mutagenic studies, the derived structure of orexin-A provides us with a structure-functional view for novel drug design.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-R02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R02 OCA].
+R02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R02 OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Single protein]]
 [[Category: Hong, E.]]
-[[Category: Kim, H.Y.]]
+[[Category: Kim, H Y.]]
-[[Category: Kim, J.I.]]
+[[Category: Kim, J I.]]
 [[Category: Lee, W.]]
 [[Category: helix-loop-helix]]
 [[Category: turn]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:58:02 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:31 2008''