3b71: Difference between revisions

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[[Image:3b71.jpg|left|200px]]
[[Image:3b71.jpg|left|200px]]


{{Structure
<!--
|PDB= 3b71 |SIZE=350|CAPTION= <scene name='initialview01'>3b71</scene>, resolution 2.82&Aring;
The line below this paragraph, containing "STRUCTURE_3b71", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] </span>
or leave the SCENE parameter empty for the default display.
|GENE= PTK2, FAK, FAK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
-->
|DOMAIN=
{{STRUCTURE_3b71|  PDB=3b71 |  SCENE= }}  
|RELATEDENTRY=[[1k04|1K04]], [[1k05|1K05]], [[1ow6|1OW6]], [[1ow7|1OW7]], [[1ow8|1OW8]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b71 OCA], [http://www.ebi.ac.uk/pdbsum/3b71 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b71 RCSB]</span>
}}


'''CD4 endocytosis motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase'''
'''CD4 endocytosis motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase'''
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[[Category: Arold, S T.]]
[[Category: Arold, S T.]]
[[Category: Garron, M L.]]
[[Category: Garron, M L.]]
[[Category: acetylation]]
[[Category: Acetylation]]
[[Category: alternative splicing]]
[[Category: Alternative splicing]]
[[Category: atp-binding]]
[[Category: Atp-binding]]
[[Category: cell junction]]
[[Category: Cell junction]]
[[Category: four-helix bundle]]
[[Category: Four-helix bundle]]
[[Category: glycoprotein]]
[[Category: Glycoprotein]]
[[Category: host-virus interaction]]
[[Category: Host-virus interaction]]
[[Category: immune response]]
[[Category: Immune response]]
[[Category: immunoglobulin domain]]
[[Category: Immunoglobulin domain]]
[[Category: kinase]]
[[Category: Kinase]]
[[Category: lipoprotein]]
[[Category: Lipoprotein]]
[[Category: membrane]]
[[Category: Membrane]]
[[Category: nucleotide-binding]]
[[Category: Nucleotide-binding]]
[[Category: palmitate]]
[[Category: Palmitate]]
[[Category: phosphorylation]]
[[Category: Phosphorylation]]
[[Category: polymorphism]]
[[Category: Polymorphism]]
[[Category: protein binding]]
[[Category: Protein binding]]
[[Category: protein-protein complex]]
[[Category: Protein-protein complex]]
[[Category: transferase]]
[[Category: Transferase]]
[[Category: transmembrane]]
[[Category: Transmembrane]]
[[Category: tyrosine-protein kinase]]
[[Category: Tyrosine-protein kinase]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:23:42 2008''

Revision as of 20:27, 4 May 2008

File:3b71.jpg

Template:STRUCTURE 3b71

CD4 endocytosis motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase


OverviewOverview

Focal adhesion kinase (FAK) and CD4 fulfil vital functions in cellular signal transduction: FAK is a central component in integrin signalling, whereas CD4 plays essential roles in the immune defence. In T lymphocytes, FAK and CD4 localise to the same signalling complexes after stimulation by either the human immunodeficiency virus (HIV) gp120 glycoprotein or an antigen, suggesting the concerted action of FAK and CD4 in these cells. Using crystallography and microcalorimetry, we here show that the focal adhesion targeting (FAT) domain of FAK binds specifically to the CD4 endocytosis motif in vitro. This FAT-CD4 complex is structurally and thermodynamically similar to the one FAT forms with paxillin LD motifs. The CD4 binding site on FAT presents the same features as the established CD4 binding site on the HIV-1 Nef protein. The binding of FAT to CD4 is incompatible with the binding of Lck to CD4. We further show that HIV-1 gp120 triggers the association of CD4 with FAK in T cells, under conditions that are known to dissociate Lck from CD4. Our results suggest that the FAK-CD4 complex represents an alternative route for eliciting T-cell-specific signals and that it links gp120 engagement to distinctive T-cell signalling during HIV infection. In infected cells, HIV-1 Nef may displace FAK from CD4 to protect the cells from apoptosis.

About this StructureAbout this Structure

3B71 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the interaction between focal adhesion kinase and CD4., Garron ML, Arthos J, Guichou JF, McNally J, Cicala C, Arold ST, J Mol Biol. 2008 Feb 1;375(5):1320-8. Epub 2007 Nov 22. PMID:18078954 Page seeded by OCA on Sun May 4 20:27:30 2008

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