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New page: left|200px<br /> <applet load="1jwf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jwf, resolution 2.100Å" /> '''Crystal Structure ...
 
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[[Image:1jwf.gif|left|200px]]<br />
[[Image:1jwf.gif|left|200px]]<br /><applet load="1jwf" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1jwf" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1jwf, resolution 2.100&Aring;" />
caption="1jwf, resolution 2.100&Aring;" />
'''Crystal Structure of human GGA1 VHS domain.'''<br />
'''Crystal Structure of human GGA1 VHS domain.'''<br />


==Overview==
==Overview==
GGAs (Golgi-localizing, gamma-adaptin ear homology domain, ARF-interacting, proteins) are critical for the transport of soluble proteins from the, trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions, with TGN-sorting receptors, ADP-ribosylation factor (ARF), and clathrin., The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic, domains of sorting receptors by recognizing acidic-cluster dileucine, (ACLL) sequences. Here we report the X-ray structure of the GGA1 VHS, domain alone, and in complex with the carboxy-terminal peptide of, cation-independent mannose 6-phosphate receptor containing an ACLL, sequence. The VHS domain forms a super helix with eight alpha-helices, similar to the VHS domains of TOM1 and Hrs. Unidirectional movements of, helices alpha6 and alpha8, and some of their side chains, create a set of, electrostatic and hydrophobic interactions for correct recognition of the, ACLL peptide. This recognition mechanism provides the basis for regulation, of protein transport from the TGN to endosomes/lysosomes, which is shared, by sortilin and low-density lipoprotein receptor-related protein.
GGAs (Golgi-localizing, gamma-adaptin ear homology domain, ARF-interacting proteins) are critical for the transport of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF), and clathrin. The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster dileucine (ACLL) sequences. Here we report the X-ray structure of the GGA1 VHS domain alone, and in complex with the carboxy-terminal peptide of cation-independent mannose 6-phosphate receptor containing an ACLL sequence. The VHS domain forms a super helix with eight alpha-helices, similar to the VHS domains of TOM1 and Hrs. Unidirectional movements of helices alpha6 and alpha8, and some of their side chains, create a set of electrostatic and hydrophobic interactions for correct recognition of the ACLL peptide. This recognition mechanism provides the basis for regulation of protein transport from the TGN to endosomes/lysosomes, which is shared by sortilin and low-density lipoprotein receptor-related protein.


==About this Structure==
==About this Structure==
1JWF 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=1JWF OCA].  
1JWF 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=1JWF OCA].  


==Reference==
==Reference==
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[[Category: super helix]]
[[Category: super helix]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:30 2008''