1u5s: Difference between revisions

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New page: left|200px<br /> <applet load="1u5s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u5s" /> '''NMR structure of the complex between Nck-2 ...
 
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[[Image:1u5s.gif|left|200px]]<br />
[[Image:1u5s.gif|left|200px]]<br /><applet load="1u5s" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1u5s" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1u5s" />
caption="1u5s" />
'''NMR structure of the complex between Nck-2 SH3 domain and PINCH-1 LIM4 domain'''<br />
'''NMR structure of the complex between Nck-2 SH3 domain and PINCH-1 LIM4 domain'''<br />


==Overview==
==Overview==
Weak protein-protein interactions (PPIs) (K(D) &gt; 10(-6) M) are critical, determinants of many biological processes. However, in contrast to a large, growing number of well-characterized, strong PPIs, the weak PPIs, especially those with K(D) &gt; 10(-4) M, are poorly explored. Genome wide, there exist few 3D structures of weak PPIs with K(D) &gt; 10(-4) M, and none, with K(D) &gt; 10(-3) M. Here, we report the NMR structure of an extremely, weak focal adhesion complex (K(D) approximately 3 x 10(-3) M) between, Nck-2 SH3 domain and PINCH-1 LIM4 domain. The structure exhibits a, remarkably small and polar interface with distinct binding modes for both, SH3 and LIM domains. Such an interface suggests a transient Nck-2/PINCH-1, association process that may trigger rapid focal adhesion turnover during, integrin signaling. Genetic rescue experiments demonstrate that this, interface is indeed involved in mediating cell shape change and migration., Together, the data provide a molecular basis for an ultraweak PPI in, regulating focal adhesion dynamics during integrin signaling.
Weak protein-protein interactions (PPIs) (K(D) &gt; 10(-6) M) are critical determinants of many biological processes. However, in contrast to a large growing number of well-characterized, strong PPIs, the weak PPIs, especially those with K(D) &gt; 10(-4) M, are poorly explored. Genome wide, there exist few 3D structures of weak PPIs with K(D) &gt; 10(-4) M, and none with K(D) &gt; 10(-3) M. Here, we report the NMR structure of an extremely weak focal adhesion complex (K(D) approximately 3 x 10(-3) M) between Nck-2 SH3 domain and PINCH-1 LIM4 domain. The structure exhibits a remarkably small and polar interface with distinct binding modes for both SH3 and LIM domains. Such an interface suggests a transient Nck-2/PINCH-1 association process that may trigger rapid focal adhesion turnover during integrin signaling. Genetic rescue experiments demonstrate that this interface is indeed involved in mediating cell shape change and migration. Together, the data provide a molecular basis for an ultraweak PPI in regulating focal adhesion dynamics during integrin signaling.


==About this Structure==
==About this Structure==
1U5S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U5S OCA].  
1U5S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U5S OCA].  


==Reference==
==Reference==
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[[Category: zinc finger]]
[[Category: zinc finger]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:31:59 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:57 2008''