1tfj: Difference between revisions

Revision as of 00:20, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1tfj.png

Template:STRUCTURE 1tfj

Crystal structure of Bovine Glycolipid transfer protein in complex with a fatty acidCrystal structure of Bovine Glycolipid transfer protein in complex with a fatty acid

Template:ABSTRACT PUBMED 16309699

About this StructureAbout this Structure

1TFJ is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structural evidence for adaptive ligand binding of glycolipid transfer protein., Airenne TT, Kidron H, Nymalm Y, Nylund M, West G, Mattjus P, Salminen TA, J Mol Biol. 2006 Jan 13;355(2):224-36. Epub 2005 Nov 8. PMID:16309699

Page seeded by OCA on Tue Jul 29 00:20:27 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of Bovine Glycolipid transfer protein in complex with a fatty acid'''
+===Crystal structure of Bovine Glycolipid transfer protein in complex with a fatty acid===
-==Overview==
+<!--
-Glycolipids participate in many important cellular processes and they are bound and transferred with high specificity by glycolipid transfer protein (GLTP). We have solved three different X-ray structures of bovine GLTP at 1.4 angstroms, 1.6 angstroms and 1.8 angstroms resolution, all with a bound fatty acid or glycolipid. The 1.4 angstroms structure resembles the recently characterized apo-form of the human GLTP but the other two structures represent an intermediate conformation of the apo-GLTPs and the human lactosylceramide-bound GLTP structure. These novel structures give insight into the mechanism of lipid binding and how GLTP may conformationally adapt to different lipids. Furthermore, based on the structural comparison of the GLTP structures and the three-dimensional models of the related Podospora anserina HET-C2 and Arabidopsis thaliana accelerated cell death protein, ACD11, we give structural explanations for their specific lipid binding properties.
+The line below this paragraph, {{ABSTRACT_PUBMED_16309699}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16309699 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16309699}}
 ==About this Structure==
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 [[Category: Glycolipid]]
 [[Category: Lipid transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:53:29 2008''
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