2bjn
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(New page: 200px<br /> <applet load="2bjn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bjn, resolution 1.70Å" /> '''X-RAY STRUCTURE OF ...)
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Revision as of 18:13, 29 October 2007
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X-RAY STRUCTURE OF HUMAN TPC6
Overview
The TRAPP (transport protein particle) complexes are tethering complexes, that have an important role at the different steps of vesicle transport., Recently, the crystal structures of the TRAPP subunits SEDL and BET3 have, been determined, and we present here the 1.7 Angstroms crystal structure, of human TPC6, a third TRAPP subunit. The protein adopts an, alpha/beta-plait topology and forms a dimer. In spite of low sequence, similarity, the structure of TPC6 strikingly resembles that of BET3. The, similarity is especially prominent at the dimerization interfaces of the, proteins. This suggests heterodimerization of TPC6 and BET3, which is, shown by in vitro and in vivo association studies. Together with TPC5, another TRAPP subunit, TPC6 and BET3 are supposed to constitute a family, of ... [(full description)]
About this Structure
2BJN is a [Single protein] structure of sequence from [Homo sapiens] with SO4 and GOL as [ligands]. Full crystallographic information is available from [OCA].
Reference
The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP subcomplex., Kummel D, Muller JJ, Roske Y, Misselwitz R, Bussow K, Heinemann U, EMBO Rep. 2005 Aug;6(8):787-93. PMID:16025134
Page seeded by OCA on Mon Oct 29 20:18:34 2007
Categories: Homo sapiens | Single protein | Bussow, K. | Heinemann, U. | Kummel, D. | Misselwitz, R. | Mueller, J.J. | Roske, Y. | GOL | SO4 | Tethering | Tpc6 | Transport protein | Trapp complex