Structural highlights
Function
BAP29_HUMAN May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8-mediated apoptosis (By similarity).
Publication Abstract from PubMed
The vDED coiled coil domain from human BAP29 was crystallized in dimeric and tetrameric forms. For the dimer, a disulfide bond was unexpectedly found to bridge a crystal contact, resulting in complete cross-linking along the c-axis. This indicates that it is in principle possible to design spontaneously polymerizing protein crystals.
A disulfide polymerized protein crystal.,Quistgaard EM Chem Commun (Camb). 2014 Oct 20. PMID:25327138[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Quistgaard EM. A disulfide polymerized protein crystal. Chem Commun (Camb). 2014 Oct 20. PMID:25327138 doi:http://dx.doi.org/10.1039/c4cc07326f
