1ri9
From Proteopedia
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| - | [[Image:1ri9.gif|left|200px]] | + | [[Image:1ri9.gif|left|200px]] |
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| - | '''Structure of a helically extended SH3 domain of the T cell adapter protein ADAP''' | + | {{Structure |
| + | |PDB= 1ri9 |SIZE=350|CAPTION= <scene name='initialview01'>1ri9</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= FYB, SLAP130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of a helically extended SH3 domain of the T cell adapter protein ADAP''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RI9 is a [ | + | 1RI9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RI9 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of a helically extended SH3 domain of the T cell adapter protein ADAP., Heuer K, Kofler M, Langdon G, Thiemke K, Freund C, Structure. 2004 Apr;12(4):603-10. PMID:[http:// | + | Structure of a helically extended SH3 domain of the T cell adapter protein ADAP., Heuer K, Kofler M, Langdon G, Thiemke K, Freund C, Structure. 2004 Apr;12(4):603-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15062083 15062083] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sh3-like]] | [[Category: sh3-like]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:52:04 2008'' |
Revision as of 11:52, 20 March 2008
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| Gene: | FYB, SLAP130 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of a helically extended SH3 domain of the T cell adapter protein ADAP
Overview
The adapter protein ADAP (FYB/SLAP-130) provides a critical link between T cell receptor (TCR) signaling and cell adhesion via the activation of integrins. The C-terminal 70 residues of ADAP show homology to SH3 domains; however, conserved residues of the fold are absent. An alignment and annotation of this domain has therefore been elusive. We have solved the three-dimensional structure of the ADAP C-terminal domain by NMR spectroscopy and show that it represents an altered SH3 domain fold. An N-terminal, amphipathic helix makes extensive contacts to residues of the regular SH3 domain fold, and thereby a composite surface with unusual surface properties is created. We propose this SH3 domain variant to be classified as a helically extended SH3 domain (hSH3 domain) and show that the ADAP-hSH3 domain can no longer bind conventional proline-rich peptides.
About this Structure
1RI9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a helically extended SH3 domain of the T cell adapter protein ADAP., Heuer K, Kofler M, Langdon G, Thiemke K, Freund C, Structure. 2004 Apr;12(4):603-10. PMID:15062083
Page seeded by OCA on Thu Mar 20 13:52:04 2008
