1ft1: Difference between revisions

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[[Image:1ft1.gif|left|200px]]<br /><applet load="1ft1" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ft1.gif|left|200px]]<br /><applet load="1ft1" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ft1, resolution 2.25Å" />

'''CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION'''<br />

==Overview==

Protein farnesyltransferase (FTase) catalyzes the carboxyl-terminal, lipidation of Ras and several other cellular signal transduction proteins., The essential nature of this modification for proper function of these, proteins has led to the emergence of FTase as a target for the development, of new anticancer therapy. Inhibition of this enzyme suppresses the, transformed phenotype in cultured cells and causes tumor regression in, animal models. The crystal structure of heterodimeric mammalian FTase was, determined at 2.25 angstrom resolution. The structure shows a combination, of two unusual domains: a crescent-shaped seven-helical hairpin domain and, an alpha-alpha barrel domain. The active site is formed by two clefts that, intersect at a bound zinc ion. One cleft contains a nine-residue peptide, that may mimic the binding of the Ras substrate; the other cleft is lined, with highly conserved aromatic residues appropriate for binding the, farnesyl isoprenoid with required specificity.

Protein farnesyltransferase (FTase) catalyzes the carboxyl-terminal lipidation of Ras and several other cellular signal transduction proteins. The essential nature of this modification for proper function of these proteins has led to the emergence of FTase as a target for the development of new anticancer therapy. Inhibition of this enzyme suppresses the transformed phenotype in cultured cells and causes tumor regression in animal models. The crystal structure of heterodimeric mammalian FTase was determined at 2.25 angstrom resolution. The structure shows a combination of two unusual domains: a crescent-shaped seven-helical hairpin domain and an alpha-alpha barrel domain. The active site is formed by two clefts that intersect at a bound zinc ion. One cleft contains a nine-residue peptide that may mimic the binding of the Ras substrate; the other cleft is lined with highly conserved aromatic residues appropriate for binding the farnesyl isoprenoid with required specificity.

==About this Structure==

1FT1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1FT1 OCA].

1FT1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FT1 OCA].

==Reference==

Line 13:

[[Category: Protein complex]]

[[Category: Rattus norvegicus]]

[[Category: Beese, L.S.]]

[[Category: Beese, L S.]]

[[Category: Park, H.W.]]

[[Category: Park, H W.]]

[[Category: ZN]]

[[Category: cancer therapeutics]]

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[[Category: transferase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 15~~:15:~~04 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:20 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ft1.gif|left|200px]]<br /><applet load="1ft1" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ft1.gif|left|200px]]<br /><applet load="1ft1" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ft1, resolution 2.25&Aring;" />
 '''CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION'''<br />
 ==Overview==
-Protein farnesyltransferase (FTase) catalyzes the carboxyl-terminal, lipidation of Ras and several other cellular signal transduction proteins., The essential nature of this modification for proper function of these, proteins has led to the emergence of FTase as a target for the development, of new anticancer therapy. Inhibition of this enzyme suppresses the, transformed phenotype in cultured cells and causes tumor regression in, animal models. The crystal structure of heterodimeric mammalian FTase was, determined at 2.25 angstrom resolution. The structure shows a combination, of two unusual domains: a crescent-shaped seven-helical hairpin domain and, an alpha-alpha barrel domain. The active site is formed by two clefts that, intersect at a bound zinc ion. One cleft contains a nine-residue peptide, that may mimic the binding of the Ras substrate; the other cleft is lined, with highly conserved aromatic residues appropriate for binding the, farnesyl isoprenoid with required specificity.
+Protein farnesyltransferase (FTase) catalyzes the carboxyl-terminal lipidation of Ras and several other cellular signal transduction proteins. The essential nature of this modification for proper function of these proteins has led to the emergence of FTase as a target for the development of new anticancer therapy. Inhibition of this enzyme suppresses the transformed phenotype in cultured cells and causes tumor regression in animal models. The crystal structure of heterodimeric mammalian FTase was determined at 2.25 angstrom resolution. The structure shows a combination of two unusual domains: a crescent-shaped seven-helical hairpin domain and an alpha-alpha barrel domain. The active site is formed by two clefts that intersect at a bound zinc ion. One cleft contains a nine-residue peptide that may mimic the binding of the Ras substrate; the other cleft is lined with highly conserved aromatic residues appropriate for binding the farnesyl isoprenoid with required specificity.
 ==About this Structure==
-FT1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FT1 OCA].
+FT1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FT1 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Rattus norvegicus]]
-[[Category: Beese, L.S.]]
+[[Category: Beese, L S.]]
-[[Category: Park, H.W.]]
+[[Category: Park, H W.]]
 [[Category: ZN]]
 [[Category: cancer therapeutics]]
@@ Line 23: / Line 23: @@
 [[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:15:04 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:20 2008''