1lm8: Difference between revisions

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[[Image:1lm8.gif|left|200px]]<br />

[[Image:1lm8.gif|left|200px]]<br /><applet load="1lm8" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1lm8" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1lm8, resolution 1.85Å" />

'''Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex'''<br />

==Overview==

The ubiquitination of the hypoxia-inducible factor (HIF) by the von, Hippel-Lindau tumor suppressor (pVHL) plays a central role in the cellular, response to changes in oxygen availability. pVHL binds to HIF only when a, conserved proline in HIF is hydroxylated, a modification that is, oxygen-dependent. The 1.85 angstrom structure of a 20-residue HIF-1alpha, peptide-pVHL-ElonginB-ElonginC complex shows that HIF-1alpha binds to pVHL, in an extended beta strand-like conformation. The hydroxyproline inserts, into a gap in the pVHL hydrophobic core, at a site that is a hotspot for, tumorigenic mutations, with its 4-hydroxyl group recognized by buried, serine and histidine residues. Although the beta sheet-like interactions, contribute to the stability of the complex, the hydroxyproline contacts, are central to the strict specificity characteristic of signaling.

The ubiquitination of the hypoxia-inducible factor (HIF) by the von Hippel-Lindau tumor suppressor (pVHL) plays a central role in the cellular response to changes in oxygen availability. pVHL binds to HIF only when a conserved proline in HIF is hydroxylated, a modification that is oxygen-dependent. The 1.85 angstrom structure of a 20-residue HIF-1alpha peptide-pVHL-ElonginB-ElonginC complex shows that HIF-1alpha binds to pVHL in an extended beta strand-like conformation. The hydroxyproline inserts into a gap in the pVHL hydrophobic core, at a site that is a hotspot for tumorigenic mutations, with its 4-hydroxyl group recognized by buried serine and histidine residues. Although the beta sheet-like interactions contribute to the stability of the complex, the hydroxyproline contacts are central to the strict specificity characteristic of signaling.

==Disease==

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==About this Structure==

1LM8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1LM8 OCA].

1LM8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LM8 OCA].

==Reference==

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[[Category: Gertler, F.]]

[[Category: Ivan, M.]]

[[Category: JR., W.G.Kaelin.]]

[[Category: JR., W G.Kaelin.]]

[[Category: Min, J-H]]

[[Category: Pavletich, N.P.]]

[[Category: Pavletich, N P.]]

[[Category: Yang, H.]]

[[Category: oxygen sensing]]

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[[Category: tumor suppressor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 18~~:02:~~30 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:15 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1lm8.gif|left|200px]]<br />
+[[Image:1lm8.gif|left|200px]]<br /><applet load="1lm8" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1lm8" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1lm8, resolution 1.85&Aring;" />
 '''Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex'''<br />
 ==Overview==
-The ubiquitination of the hypoxia-inducible factor (HIF) by the von, Hippel-Lindau tumor suppressor (pVHL) plays a central role in the cellular, response to changes in oxygen availability. pVHL binds to HIF only when a, conserved proline in HIF is hydroxylated, a modification that is, oxygen-dependent. The 1.85 angstrom structure of a 20-residue HIF-1alpha, peptide-pVHL-ElonginB-ElonginC complex shows that HIF-1alpha binds to pVHL, in an extended beta strand-like conformation. The hydroxyproline inserts, into a gap in the pVHL hydrophobic core, at a site that is a hotspot for, tumorigenic mutations, with its 4-hydroxyl group recognized by buried, serine and histidine residues. Although the beta sheet-like interactions, contribute to the stability of the complex, the hydroxyproline contacts, are central to the strict specificity characteristic of signaling.
+The ubiquitination of the hypoxia-inducible factor (HIF) by the von Hippel-Lindau tumor suppressor (pVHL) plays a central role in the cellular response to changes in oxygen availability. pVHL binds to HIF only when a conserved proline in HIF is hydroxylated, a modification that is oxygen-dependent. The 1.85 angstrom structure of a 20-residue HIF-1alpha peptide-pVHL-ElonginB-ElonginC complex shows that HIF-1alpha binds to pVHL in an extended beta strand-like conformation. The hydroxyproline inserts into a gap in the pVHL hydrophobic core, at a site that is a hotspot for tumorigenic mutations, with its 4-hydroxyl group recognized by buried serine and histidine residues. Although the beta sheet-like interactions contribute to the stability of the complex, the hydroxyproline contacts are central to the strict specificity characteristic of signaling.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-LM8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LM8 OCA].
+LM8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LM8 OCA].
 ==Reference==
@@ Line 19: / Line 18: @@
 [[Category: Gertler, F.]]
 [[Category: Ivan, M.]]
-[[Category: JR., W.G.Kaelin.]]
+[[Category: JR., W G.Kaelin.]]
 [[Category: Min, J-H]]
-[[Category: Pavletich, N.P.]]
+[[Category: Pavletich, N P.]]
 [[Category: Yang, H.]]
 [[Category: oxygen sensing]]
@@ Line 27: / Line 26: @@
 [[Category: tumor suppressor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:02:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:15 2008''