1jwf: Difference between revisions

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[[Image:1jwf.gif|left|200px]]
{{Seed}}
[[Image:1jwf.png|left|200px]]


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{{STRUCTURE_1jwf|  PDB=1jwf  |  SCENE=  }}  
{{STRUCTURE_1jwf|  PDB=1jwf  |  SCENE=  }}  


'''Crystal Structure of human GGA1 VHS domain.'''
===Crystal Structure of human GGA1 VHS domain.===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_11859376}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11859376 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11859376}}


==About this Structure==
==About this Structure==
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[[Category: Wakatsuki, S.]]
[[Category: Wakatsuki, S.]]
[[Category: Super helix]]
[[Category: Super helix]]
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