1ri9: Difference between revisions

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="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1ri9" />

'''Structure of a helically extended SH3 domain of the T cell adapter protein ADAP'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1RI9 OCA].

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==

Line 22:

Line 21:

[[Category: sh3-like]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 19~~:04:~~13 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:10 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ 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="450" color="white" frame="true" align="right" spinBox="true"
 caption="1ri9" />
 '''Structure of a helically extended SH3 domain of the T cell adapter protein ADAP'''<br />
 ==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.
+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==
-RI9 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RI9 OCA].
+RI9 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==
@@ Line 22: / Line 21: @@
 [[Category: sh3-like]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:04:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:10 2008''