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10.1073/pnas.1719709115 http://scihub22266oqcxt.onion/10.1073/pnas.1719709115 C5798383!5798383!29339490     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2018 ; 115 (5): E856-65 Nephropedia Template TP {{tp|p=29339490|t=2018. Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites |pdf=|usr=}}{{29339490}} gab.com Text Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29339490 #FOAvip Intracellular sterol distribution mediated by lipid transfer proteins (LTPs) is crucial for membrane function. LTPs anchored at membrane contact sites (LAMs), new members of LTPs in the StARkin superfamily, have sterol transport roles at contact sites between the endoplasmic reticulum (ER) and other membranes. The determinants for ligand specificity and protein targeting were elusive. Here, we determined the structures of the pleckstrin homology (PH)-like domain and the StARkin domains from LAM homologs. The Lam6 PH-like domain has a unique PH domain fold critical for targeting to ER?mitochondrial contacts. The LAM StARkin domains have a hydrophobic cavity that accommodates a sterol ligand. This work provides a structural explanation for the sterol recognition of LAMs, which can be extended to understand the sterol-binding mode of other LTPs in the StARkin superfamily. Twit Text FOAVip Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29339490 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29339490 #FOAvip English Wikipedia <ref>{{Cite pmid|29339490}}</ref> Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites #MMPMID29339490 Tong J; Manik MK; Im YJ Proc Natl Acad Sci U S A 2018[Jan]; 115 (5): E856-65 PMID29339490show ga Intracellular sterol distribution mediated by lipid transfer proteins (LTPs) is crucial for membrane function. LTPs anchored at membrane contact sites (LAMs), new members of LTPs in the StARkin superfamily, have sterol transport roles at contact sites between the endoplasmic reticulum (ER) and other membranes. The determinants for ligand specificity and protein targeting were elusive. Here, we determined the structures of the pleckstrin homology (PH)-like domain and the StARkin domains from LAM homologs. The Lam6 PH-like domain has a unique PH domain fold critical for targeting to ER?mitochondrial contacts. The LAM StARkin domains have a hydrophobic cavity that accommodates a sterol ligand. This work provides a structural explanation for the sterol recognition of LAMs, which can be extended to understand the sterol-binding mode of other LTPs in the StARkin superfamily. äStructural basis of sterol recognition and nonvesicular transport by l(epmc).pdf DeepDyve Pubget Overpricing