Structure of a second crystal form of bence-jones protein loc

Strikingly different domain associations in two crystal forms of a single protein

M. Schiffer, C. Ainsworth, Z. B. Xu, W. Carperos, K. Olsen, Alan Solomon, F. J. Stevens, C. H. Chang

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

We have determined the structure of the immunoglobulin light-chain dimer Loc in a second crystal form that was grown from distilled water. The crystal structure was determined to 2.8-A resolution; the R factor is 0.22. The two variable domains are related by local 2-fold axes and form an antigen binding “pocket”. The variable domain-variable domain interaction observed in this crystal form differs from the one exhibited by the protein when crystallized from ammonium sulfate in which the two variable domains formed a protrusion (Chang et al., 1985). The structure attained in the distilled water crystals is similar to, but not identical with, the one observed for the Mcg light-chain dimer in crystals grown from ammonium sulfate. Thus, two strikingly different structures were attained by this multisubunit protein in crystals grown under two different, commonly used, crystallization techniques. The quaternary interactions exhibited by the protein in the two crystal forms are sufficiently different to suggest fundamentally different interpretations of the structural basis for the function of this protein. This observation may have general implications regarding the use of single crystallographic determinations for detailed identification of structural and functional relationships. On the other hand, proteins whose structures can be altered by manipulation of crystallization conditions may provide useful systems for study of fundamental structural chemistry.

Original languageEnglish (US)
Pages (from-to)4066-4072
Number of pages7
JournalBiochemistry
Volume28
Issue number9
DOIs
StatePublished - Jan 1 1989

Fingerprint

Bence Jones Protein
Crystals
Ammonium Sulfate
Crystallization
Proteins
Dimers
Immunoglobulin Light Chains
Water
R Factors
Light
Antigens
Crystal structure

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Structure of a second crystal form of bence-jones protein loc : Strikingly different domain associations in two crystal forms of a single protein. / Schiffer, M.; Ainsworth, C.; Xu, Z. B.; Carperos, W.; Olsen, K.; Solomon, Alan; Stevens, F. J.; Chang, C. H.

In: Biochemistry, Vol. 28, No. 9, 01.01.1989, p. 4066-4072.

Research output: Contribution to journalArticle

Schiffer, M. ; Ainsworth, C. ; Xu, Z. B. ; Carperos, W. ; Olsen, K. ; Solomon, Alan ; Stevens, F. J. ; Chang, C. H. / Structure of a second crystal form of bence-jones protein loc : Strikingly different domain associations in two crystal forms of a single protein. In: Biochemistry. 1989 ; Vol. 28, No. 9. pp. 4066-4072.
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N2 - We have determined the structure of the immunoglobulin light-chain dimer Loc in a second crystal form that was grown from distilled water. The crystal structure was determined to 2.8-A resolution; the R factor is 0.22. The two variable domains are related by local 2-fold axes and form an antigen binding “pocket”. The variable domain-variable domain interaction observed in this crystal form differs from the one exhibited by the protein when crystallized from ammonium sulfate in which the two variable domains formed a protrusion (Chang et al., 1985). The structure attained in the distilled water crystals is similar to, but not identical with, the one observed for the Mcg light-chain dimer in crystals grown from ammonium sulfate. Thus, two strikingly different structures were attained by this multisubunit protein in crystals grown under two different, commonly used, crystallization techniques. The quaternary interactions exhibited by the protein in the two crystal forms are sufficiently different to suggest fundamentally different interpretations of the structural basis for the function of this protein. This observation may have general implications regarding the use of single crystallographic determinations for detailed identification of structural and functional relationships. On the other hand, proteins whose structures can be altered by manipulation of crystallization conditions may provide useful systems for study of fundamental structural chemistry.

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