Crystal structure of recombinant rabbit interferon-gamma at 2.7-A resolution.

Samudzi, Cleopas T.; Burton, Louis E.; Rubin, John R.

doi:10.1016/s0021-9258(18)54706-2

Cited by 71 publications

(10 citation statements)

References 24 publications

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“…Here we report the 2.0 A crystal structure of recombinant human . Unexpectedly, rhIL-10 exists as an intercalated dimer as first observed for IFN-y (Ealick et al, 1991;Samudzi et al, 1991). Comparison of IL-10 and IFN-y reveals a conserved fiveresidue core which is conserved in all species of both cytokines.…”

mentioning

confidence: 68%

“…the crystal and NMR structures of IFN-y have shown the AB loop to be highly flexible with no clear secondary structure (Ealick et al. 1991;Samudzi et al, 1991;Grzesiek et al, 1992). This is noteworthy since the AB loop of IFN-y has been show n to interact with the IFN-y receptor ) and the loops are in close proximity with the structurally conserved bend in helix F'.…”

Section: Discussionmentioning

confidence: 99%

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Crystal Structure of Interleukin 10 Reveals an Interferon .gamma.-like Fold

Walter¹,

Nagabhushan²

1995

Biochemistry

131

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The crystal structure of recombinant human interleukin 10 (rhIL-10) has been determined by X-ray crystallography at 2.0 A resolution. Interleukin 10 is a dimer composed of identical polypeptide chains related by a 2-fold axis. The molecule is predominantly alpha-helical. The main-chain fold resembles that of interferon gamma (IFN-gamma) in which the structural integrity of each domain is dependent on the intertwining of helices from each peptide chain. Comparison of rhIL-10 and IFN-gamma reveals differences in helix lengths and orientations of the 2-fold related domains. Interleukin 10 and IFN-gamma contain several conserved residues in their internal cores which suggest a possible "fingerprint" for detection of other members of this fold.

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mentioning

confidence: 68%

Section: Discussionmentioning

confidence: 99%

Crystal Structure of Interleukin 10 Reveals an Interferon .gamma.-like Fold

Walter¹,

Nagabhushan²

1995

Biochemistry

131

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“…The coding sequence for the mature human IFNcomprises 143 amino acids (Ealick et al, 1991;Samudzi et al, 1991). Crystallographic studies on human IFN-(3.5-Á resolution; Ealick et al, 1991) and rabbit IFN-(2.7-Á resolution; Samudzi et al, 1991) confirmed the high a-helical content of 60-70% which had been predicted on the basis of ultraviolet circular dichroism (Hogrefe etal., 1989;Arakawa et al, 1987). Both crystal structures show the same overall motif where four of the six helices of one monomer form a cleft that accommodates the last helix of the second monomer.…”

mentioning

confidence: 71%

Proton, carbon-13, and nitrogen-15 NMR backbone assignments and secondary structure of human interferon-.gamma.

Grzesiek¹,

Döbeli²,

Gentz³

et al. 1992

Biochemistry

158

109

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1H, 13C, and 15N NMR assignments of the protein backbone of human interferon-gamma, a homodimer of 31.4 kDa, have been made using the recently introduced three-dimensional (3D) triple-resonance NMR techniques. It is shown that, despite the approximately 40-50-Hz 13C alpha and 1H alpha line widths of this high molecular weight dimer and the extensive overlap in the 1H alpha and 13C alpha spectral regions, unique sequential assignments can be made on the basis of combined use of the 3D HNCO, HNCA, HN(CO)CA, and HCACO constant-time experiments, the 15N-separated 3D NOESY-HMQC, and the 3D HOHAHA-HMQC experiments. Analysis of the 15N-separated 3D NOESY-HMQC and 13C/15N-separated four-dimensional (4D) NOESY-HMQC spectra together with the secondary C alpha and C beta chemical shifts yielded extensive secondary structure information. The NMR-derived secondary structure essentially confirms results of a recently published low-resolution crystal structure [Ealick et al. (1991) Science 252, 698-702], i.e., six helices in the monomer which are mostly alpha-helical in nature, no beta-sheets, a long flexible loop between helices A and B, and a very hydrophobic helix C. The functionally important carboxy terminus, which was not observed in the X-ray study, does not adopt a rigid conformation in solution. A high degree of internal mobility, starting at Pro-123, gives rise to significantly narrower resonance line widths for these carboxy-terminal residues compared to the rest of the protein.

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“…The architecture of the IL-10 dimer is reminiscent of that found in the structures of human [13], rabbit [30] and bovine (A Randall and A Kossiakoff, personal communication) IFNy. Figure 6a shows that it is possible to align the dimers of hIL-10 and bIFNy in a way that enhances the similarity of the shape and size of these molecules.…”

Section: Similarity To the Topological Structure Of Interferon Ymentioning

confidence: 82%

Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon γ

Zdanov

Schalk-Hihi²,

Gustchina³

et al. 1995

Structure

210

145

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The topological similarity of IL-10 to IFN gamma was totally unexpected, and may be a reflection of the close relationship between the biological effects of these two cytokines. The structure of IL-10 provides insights into the possible modes of conversion of the dimer into monomers, and of putative sites of receptor interactions. The good level of refinement and high resolution of this structure show that the internal disorder often associated with other helical cytokines is not an essential feature of this class of proteins.

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Crystal structure of recombinant rabbit interferon-gamma at 2.7-A resolution.

Cited by 71 publications

References 24 publications

Crystal Structure of Interleukin 10 Reveals an Interferon .gamma.-like Fold

Crystal Structure of Interleukin 10 Reveals an Interferon .gamma.-like Fold

Proton, carbon-13, and nitrogen-15 NMR backbone assignments and secondary structure of human interferon-.gamma.

Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon γ

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