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Accession number;06A0548454
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| Title;Studies for Intracellular Vesicular Transport and Posttranslational Protein Modification Using X-ray Crystallographic Analysis |
| Author;
SHIBA TOMOO
(Univ. Tokyo, Graduate School of Arts and Sciences, JPN)
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Journal Title;Journal of the Crystallographic Society of Japan
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Journal Code:G0232A
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ISSN:0369-4585
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VOL.48;NO.3;PAGE.207-215(2006)
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| Figure&Table&Reference;FIG.6, TBL.1, REF.24 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;GGAs (Golgi-localizing, .GAMMA.-adaptin ear homology domain, ARF-binding proteins) are a family of monomeric clathrin adaptor proteins that are conserved from yeasts to humans. The GGA molecule is composed of four functional regions:a VHS domain that interacts with TGN sorting receptors, such as mannose 6-phosphate receptors (MPR); a GAT domain that binds to the GTP-bound form of ARF; a hinge region that interacts with clathrin; a GAE domain interacts with accessory proteins. We have determined the crystal structures of VHS, GAT and AP-1 .GAMMA.-ear domain that is the homolog of GAE domain. And we have also revealed the crystal structure of glucuronyltransferase, GlcAT-P which is critical enzyme in the biosynthesis of the carbohydrate epitope HNK-1. (author abst.) |
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