GLTP

Glycolipid transfer protein

PDB rendering based on 1swx.

Available structures

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

Symbol

GLTP

External IDs

OMIM: 608949 MGI: 1929253 HomoloGene: 41133 GeneCards: GLTP Gene

Gene ontology
Molecular function	• protein binding • lipid binding • glycolipid transporter activity • glycolipid binding
Cellular component	• cytosol • membrane • extracellular exosome
Biological process	• sphingolipid metabolic process • glycosphingolipid metabolic process • small molecule metabolic process • glycolipid transport
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
109.85 – 109.88 Mb

Chr 5:
114.67 – 114.69 Mb

PubMed search

Glycolipid transfer protein is a protein that in humans is encoded by the GLTP gene.^[1]^[2]^[3]

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.^[3]

References

↑ 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.
1 2 "Entrez Gene: GLTP glycolipid transfer protein".

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. 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. 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. 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

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GLTP

References

Further reading