1vfy: Difference between revisions

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[[Image:1vfy.gif|left|200px]]
{{Seed}}
[[Image:1vfy.png|left|200px]]


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{{STRUCTURE_1vfy|  PDB=1vfy  |  SCENE=  }}  
{{STRUCTURE_1vfy|  PDB=1vfy  |  SCENE=  }}  


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




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_10367894}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10367894 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10367894}}


==About this Structure==
==About this Structure==
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[[Category: Intracellular trafficking]]
[[Category: Intracellular trafficking]]
[[Category: Transport protein]]
[[Category: Transport protein]]
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