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3CDC

kI O18/O8 N34I/Y87H immunoglobulin light chain variable domain

Summary for 3CDC
Entry DOI10.2210/pdb3cdc/pdb
Related3CDF 3CDY
DescriptorLight Chain Amyloidogenic (2 entities in total)
Functional Keywordsgreek key beta barrel, amyloid, immunoglobulin, light chain, variable domain, immune system
Biological sourceHomo sapiens
Total number of polymer chains2
Total formula weight23890.29
Authors
Baden, E.M.,Randles, E.G.,Thompson, J.R.,Ramirez-Alvarado, M. (deposition date: 2008-02-26, release date: 2008-09-02, Last modification date: 2024-10-30)
Primary citationBaden, E.M.,Randles, E.G.,Aboagye, A.K.,Thompson, J.R.,Ramirez-Alvarado, M.
Structural insights into the role of mutations in amyloidogenesis.
J.Biol.Chem., 283:30950-30956, 2008
Cited by
PubMed Abstract: Mechanisms of amyloidogenesis are not well understood, including potential structural contributions of mutations in the process. Our previous research indicated that the dimer interface of amyloidogenic immunoglobulin light chain protein AL-09 is twisted 90 degrees relative to the protein from its germline sequence, kappaI O18/O8. Here we report a systematic restoration of AL-09 to its germline sequence by mutating the non-conservative somatic mutations located in the light chain dimer interface. Among these mutants, we find a correlation between increased thermodynamic stability and an increase in the lag time for fibril formation. The restorative mutant AL-09 H87Y completes the trifecta and restores the dimer interface observed in kappaI O18/O8, emphasizing the potential importance of the structural integrity of these proteins to protect against amyloidogenicity. We also find that adding amyloidogenic mutations into the germline protein illustrates mutational cooperativity in promoting amyloidogenesis.
PubMed: 18768467
DOI: 10.1074/jbc.M804822200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.53 Å)
Structure validation

226707

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