4w7y
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Dimeric BAP29 vDED with disulfide bonds in crystal contacts
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Structural highlights
FunctionBAP29_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 PubMedThe 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
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This page was last modified 06:56, 7 April 2023.