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Protein-coding gene in humans
GLTP Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1SWX , 1SX6 , 2EUK , 2EUM , 2EVD , 2EVL , 2EVS , 2EVT , 3RIC , 3RWV , 3RZN , 3S0I , 3S0K , 4GH0 , 4GHP , 4GHS , 4GIX , 4GJQ , 4GVT , 4GXD , 4GXG , 4H2Z
Identifiers Aliases GLTP External IDs OMIM : 608949 MGI : 1929253 HomoloGene : 41133 GeneCards : GLTP Wikidata
Glycolipid transfer protein is a protein that in humans is encoded by the GLTP gene .[5] [6] [7]
The protein encoded by this gene is similar to bovine and porcine proteins which accelerate transfer of certain glycosphingolipids and glyceroglycolipids between membranes. It is thought to be a cytoplasmic protein.[7]
References [ edit ]
^ a b c GRCh38: Ensembl release 89: ENSG00000139433 – Ensembl , May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000011884 – Ensembl , May 2017^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ Li XM, Malakhova ML, Lin X, Pike HM, Chung T, Molotkovsky JG, Brown RE (Aug 2004). "Human glycolipid transfer protein: probing conformation using fluorescence spectroscopy" . Biochemistry . 43 (31): 10285–94. doi :10.1021/bi0495432 . PMC 2593833 PMID 15287756 . ^ Malakhova ML, Malinina L, Pike HM, Kanack AT, Patel DJ, Brown RE (Jul 2005). "Point mutational analysis of the liganding site in human glycolipid transfer protein. Functionality of the complex" . J Biol Chem . 280 (28): 26312–20. doi :10.1074/jbc.M500481200 PMC 1393170 PMID 15901739 . ^ a b "Entrez Gene: GLTP glycolipid transfer protein" .
Further reading [ edit ]
Brown RE, Mattjus P (2007). "Glycolipid transfer proteins" . Biochim. Biophys. Acta . 1771 (6): 746–60. doi :10.1016/j.bbalip.2007.01.011 . PMC 1986823 PMID 17320476 . Abe A (1990). "Primary structure of glycolipid transfer protein from pig brain" . J. Biol. Chem . 265 (17): 9634–7. doi :10.1016/S0021-9258(19)38716-2 PMID 2190982 . Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery" . Genome Res . 6 (9): 791–806. doi :10.1101/gr.6.9.791 PMID 8889548 . Mattjus P, Pike HM, Molotkovsky JG, Brown RE (2000). "Charged membrane surfaces impede the protein-mediated transfer of glycosphingolipids between phospholipid bilayers" . Biochemistry . 39 (5): 1067–75. doi :10.1021/bi991810u . PMC 2637181 PMID 10653652 . Lin X, Mattjus P, Pike HM, et al. (2000). "Cloning and expression of glycolipid transfer protein from bovine and porcine brain" . J. Biol. Chem . 275 (7): 5104–10. doi :10.1074/jbc.275.7.5104 PMC 2621014 PMID 10671554 . Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences" . Proc. Natl. Acad. Sci. U.S.A . 99 (26): 16899–903. Bibcode :2002PNAS...9916899M . doi :10.1073/pnas.242603899 PMC 139241 PMID 12477932 . Malinina L, Malakhova ML, Teplov A, et al. (2004). "Structural basis for glycosphingolipid transfer specificity" . Nature . 430 (7003): 1048–53. Bibcode :2004Natur.430.1048M . doi :10.1038/nature02856 . PMC 2640488 PMID 15329726 . Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)" . Genome Res . 14 (10B): 2121–7. doi :10.1101/gr.2596504 . PMC 528928 PMID 15489334 . Rao CS, Lin X, Pike HM, et al. (2004). "Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses" . Biochemistry . 43 (43): 13805–15. doi :10.1021/bi0492197 . PMC 2596630 PMID 15504043 . Rao CS, Chung T, Pike HM, Brown RE (2006). "Glycolipid transfer protein interaction with bilayer vesicles: modulation by changing lipid composition" . Biophys. J . 89 (6): 4017–28. doi :10.1529/biophysj.105.070631 . PMC 1366967 PMID 16169991 . Malinina L, Malakhova ML, Kanack AT, et al. (2006). "The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure" . PLOS Biol . 4 (11): e362. doi :10.1371/journal.pbio.0040362 PMC 1618416 PMID 17105344 .
PDB gallery
1swx : Crystal structure of a human glycolipid transfer protein in apo-form
1sx6 : Crystal structure of human Glycolipid Transfer protein in lactosylceramide-bound form
1tfj : Crystal structure of Bovine Glycolipid transfer protein in complex with a fatty acid
1wbe : X-RAY STRUCTURE OF BOVINE GLTP
2bv7 : CRYSTAL STRUCTURE OF GLTP WITH BOUND GM3
2euk : Crystal Structure of Human Glycolipid Transfer Protein complexed with 24:1 Galactosylceramide
2eum : Crystal structure of human Glycolipid Transfer Protein complexed with 8:0 Lactosylceramide
2evd : Crystal structure of human Glycolipid Transfer Protein complexed with 12:0 Lactosylceramide
2evl : Crystal structure of human Glycolipid Transfer Protein complexed with 18:2 Galactosylceramide
2evs : Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside
2evt : Crystal structure of D48V mutant of human Glycolipid Transfer Protein
