1AR2

DISULFIDE-FREE IMMUNOGLOBULIN FRAGMENT

Summary for 1AR2

• Entry DOI: 10.2210/pdb1ar2/pdb
• Descriptor: REI (2 entities in total)
• Functional Keywords: disulfide-free, immunoglobulin fragment, bence-jones, immunoglobulin
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 11921.17

Authors

Uson, I.,Bes, M.T.,Sheldrick, G.M.,Schneider, T.R.,Hartsch, T.,Fritz, H.-J. (deposition date: 1997-08-08, release date: 1997-11-12, Last modification date: 2024-05-22)

Primary citation

Uson, I.,Bes, M.T.,Sheldrick, G.M.,Schneider, T.R.,Hartsch, T.,Fritz, H.J.
X-ray crystallography reveals stringent conservation of protein fold after removal of the only disulfide bridge from a stabilized immunoglobulin variable domain.
Structure Fold.Des., 2:357-361, 1997

PubMed Abstract: Immunoglobulin domains owe a crucial fraction of their conformational stability to an invariant central disulfide bridge, the closure of which requires oxidation. Under the reducing conditions prevailing in cell cytoplasm, accumulation of soluble immunoglobulin is prohibited by its inability to acquire and maintain the native conformation. Previously, we have shown that disulfide-free immunoglobulins can be produced in Escherichia coli and purified from cytoplasmic extracts.

PubMed: 9427009
DOI: 10.1016/S1359-0278(97)00049-7

Experimental method

X-RAY DIFFRACTION (2.8 Å)