1dcq: Difference between revisions
New page: left|200px<br /><applet load="1dcq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dcq, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ... |
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[[Image:1dcq.gif|left|200px]]<br /><applet load="1dcq" size=" | [[Image:1dcq.gif|left|200px]]<br /><applet load="1dcq" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1dcq, resolution 2.1Å" /> | caption="1dcq, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ARF-GAP DOMAIN AND ANKYRIN REPEATS OF PAPBETA.'''<br /> | '''CRYSTAL STRUCTURE OF THE ARF-GAP DOMAIN AND ANKYRIN REPEATS OF PAPBETA.'''<br /> | ||
==Overview== | ==Overview== | ||
ADP ribosylation factors (ARFs), which are members of the Ras superfamily | ADP ribosylation factors (ARFs), which are members of the Ras superfamily of GTP-binding proteins, are critical components of vesicular trafficking pathways in eukaryotes. Like Ras, ARFs are active in their GTP-bound form, and their duration of activity is controlled by GTPase-activating proteins (GAPs), which assist ARFs in hydrolyzing GTP to GDP. PAPbeta, a protein that binds to and is phosphorylated by the non-receptor tyrosine kinase PYK2, contains several modular signaling domains including a pleckstrin homology domain, an SH3 domain, ankyrin repeats and an ARF-GAP domain. Sequences of ARF-GAP domains show no recognizable similarity to those of other GAPs, and contain a characteristic Cys-X(2)-Cys-X(16-17)-Cys-X(2)-Cys motif. The crystal structure of the PAPbeta ARF-GAP domain and the C-terminal ankyrin repeats has been determined at 2.1 A resolution. The ARF-GAP domain comprises a central three-stranded beta-sheet flanked by five alpha-helices, with a Zn(2+) ion coordinated by the four cysteines of the cysteine-rich motif. Four ankyrin repeats are also present, the first two of which form an extensive interface with the ARF-GAP domain. An invariant arginine and several nearby hydrophobic residues are solvent exposed and are predicted to be the site of interaction with ARFs. Site-directed mutagenesis of these residues confirms their importance in ARF-GAP activity. | ||
==About this Structure== | ==About this Structure== | ||
1DCQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1DCQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=1DCQ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Andreev, J.]] | [[Category: Andreev, J.]] | ||
[[Category: Hubbard, S | [[Category: Hubbard, S R.]] | ||
[[Category: Mandiyan, V.]] | [[Category: Mandiyan, V.]] | ||
[[Category: Schlessinger, J.]] | [[Category: Schlessinger, J.]] | ||
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[[Category: zinc-binding module]] | [[Category: zinc-binding module]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:17 2008'' | ||
Revision as of 13:15, 21 February 2008
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CRYSTAL STRUCTURE OF THE ARF-GAP DOMAIN AND ANKYRIN REPEATS OF PAPBETA.
OverviewOverview
ADP ribosylation factors (ARFs), which are members of the Ras superfamily of GTP-binding proteins, are critical components of vesicular trafficking pathways in eukaryotes. Like Ras, ARFs are active in their GTP-bound form, and their duration of activity is controlled by GTPase-activating proteins (GAPs), which assist ARFs in hydrolyzing GTP to GDP. PAPbeta, a protein that binds to and is phosphorylated by the non-receptor tyrosine kinase PYK2, contains several modular signaling domains including a pleckstrin homology domain, an SH3 domain, ankyrin repeats and an ARF-GAP domain. Sequences of ARF-GAP domains show no recognizable similarity to those of other GAPs, and contain a characteristic Cys-X(2)-Cys-X(16-17)-Cys-X(2)-Cys motif. The crystal structure of the PAPbeta ARF-GAP domain and the C-terminal ankyrin repeats has been determined at 2.1 A resolution. The ARF-GAP domain comprises a central three-stranded beta-sheet flanked by five alpha-helices, with a Zn(2+) ion coordinated by the four cysteines of the cysteine-rich motif. Four ankyrin repeats are also present, the first two of which form an extensive interface with the ARF-GAP domain. An invariant arginine and several nearby hydrophobic residues are solvent exposed and are predicted to be the site of interaction with ARFs. Site-directed mutagenesis of these residues confirms their importance in ARF-GAP activity.
About this StructureAbout this Structure
1DCQ is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein beta., Mandiyan V, Andreev J, Schlessinger J, Hubbard SR, EMBO J. 1999 Dec 15;18(24):6890-8. PMID:10601011
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