2kd2 | pdb_00002kd2
NMR Structure of FAIM-CTD
Structural highlights
Function[FAIM1_MOUSE] Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFas apoptosis inhibitory molecule (FAIM) is a soluble cytosolic protein inhibitor of programmed cell death and is found in organisms throughout the animal kingdom. A short isoform of FAIM is expressed in all tissue types, while an alternatively spliced long isoform is specifically expressed in the brain. Here, the short isoform is shown to consist of two independently folding domains in contact with each other. The NMR solution structure of the C-terminal domain of murine FAIM is solved in isolation and revealed to be a novel protein fold, a noninterleaved seven-stranded beta-sandwich. The structure and sequence reveal several residues that are likely to be involved in functionally significant interactions with the N-terminal domain or other binding partners. Chemical shift perturbation is used to elucidate contacts made between the N-terminal domain and the C-terminal domain. Fas Apoptosis Inhibitory Molecule Contains a Novel beta-Sandwich in Contact with a Partially Ordered Domain.,Hemond M, Rothstein TL, Wagner G J Mol Biol. 2009 Jan 13. PMID:19168072[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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