1vfy: Difference between revisions

Revision as of 16:34, 21 February 2008

PHOSPHATIDYLINOSITOL-3-PHOSPHATE BINDING FYVE DOMAIN OF VPS27P PROTEIN FROM SACCHAROMYCES CEREVISIAE

OverviewOverview

Phosphatidylinositol 3-phosphate regulates membrane trafficking and signaling pathways by interacting with the FYVE domains of target proteins. The 1.15 A structure of the Vps27p FYVE domain reveals two antiparallel beta sheets and an alpha helix stabilized by two Zn2+-binding clusters. The core secondary structures are similar to a rabphilin-3A Zn2+-binding domain and to the C1 and LIM domains. Phosphatidylinositol 3-phosphate binds to a pocket formed by the (R/K)(R/K)HHCR motif. A lattice contact shows how anionic ligands can interact with the phosphatidylinositol 3-phosphate-binding site. The tip of the FYVE domain has basic and hydrophobic surfaces positioned so that nonspecific interactions with the phospholipid bilayer can abet specific binding to phosphatidylinositol 3-phosphate.

About this StructureAbout this Structure

1VFY is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p., Misra S, Hurley JH, Cell. 1999 May 28;97(5):657-66. PMID:10367894

Page seeded by OCA on Thu Feb 21 15:34:51 2008

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OCA

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-[[Image:1vfy.gif|left|200px]]<br /><applet load="1vfy" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1vfy.gif|left|200px]]<br /><applet load="1vfy" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1vfy, resolution 1.15&Aring;" />
 '''PHOSPHATIDYLINOSITOL-3-PHOSPHATE BINDING FYVE DOMAIN OF VPS27P PROTEIN FROM SACCHAROMYCES CEREVISIAE'''<br />
 ==Overview==
-Phosphatidylinositol 3-phosphate regulates membrane trafficking and, signaling pathways by interacting with the FYVE domains of target, proteins. The 1.15 A structure of the Vps27p FYVE domain reveals two, antiparallel beta sheets and an alpha helix stabilized by two Zn2+-binding, clusters. The core secondary structures are similar to a rabphilin-3A, Zn2+-binding domain and to the C1 and LIM domains. Phosphatidylinositol, 3-phosphate binds to a pocket formed by the (R/K)(R/K)HHCR motif. A, lattice contact shows how anionic ligands can interact with the, phosphatidylinositol 3-phosphate-binding site. The tip of the FYVE domain, has basic and hydrophobic surfaces positioned so that nonspecific, interactions with the phospholipid bilayer can abet specific binding to, phosphatidylinositol 3-phosphate.
+Phosphatidylinositol 3-phosphate regulates membrane trafficking and signaling pathways by interacting with the FYVE domains of target proteins. The 1.15 A structure of the Vps27p FYVE domain reveals two antiparallel beta sheets and an alpha helix stabilized by two Zn2+-binding clusters. The core secondary structures are similar to a rabphilin-3A Zn2+-binding domain and to the C1 and LIM domains. Phosphatidylinositol 3-phosphate binds to a pocket formed by the (R/K)(R/K)HHCR motif. A lattice contact shows how anionic ligands can interact with the phosphatidylinositol 3-phosphate-binding site. The tip of the FYVE domain has basic and hydrophobic surfaces positioned so that nonspecific interactions with the phospholipid bilayer can abet specific binding to phosphatidylinositol 3-phosphate.
 ==About this Structure==
-VFY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] 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=1VFY OCA].
+VFY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] 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=1VFY OCA].
 ==Reference==
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 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Hurley, J.H.]]
+[[Category: Hurley, J H.]]
 [[Category: Misra, S.]]
 [[Category: ZN]]
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 [[Category: transport protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:48:46 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:51 2008''