1ri9
From Proteopedia
(New page: 200px<br /> <applet load="1ri9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ri9" /> '''Structure of a helically extended SH3 domai...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ri9.gif|left|200px]]<br /> | + | [[Image:1ri9.gif|left|200px]]<br /><applet load="1ri9" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ri9" size=" | + | |
caption="1ri9" /> | caption="1ri9" /> | ||
'''Structure of a helically extended SH3 domain of the T cell adapter protein ADAP'''<br /> | '''Structure of a helically extended SH3 domain of the T cell adapter protein ADAP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The adapter protein ADAP (FYB/SLAP-130) provides a critical link between T | + | 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== | ==About this Structure== | ||
| - | 1RI9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1RI9 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
| Line 22: | Line 21: | ||
[[Category: sh3-like]] | [[Category: sh3-like]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:10 2008'' |
Revision as of 12:51, 21 February 2008
|
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 Feb 21 14:51:10 2008
