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1BBN

THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4 BY MULTI-DIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Summary for 1BBN
Entry DOI10.2210/pdb1bbn/pdb
DescriptorINTERLEUKIN-4 (1 entity in total)
Functional Keywordscytokine
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P05112
Total number of polymer chains1
Total formula weight15391.60
Authors
Clore, G.M.,Powers, B.,Garrett, D.S.,Gronenborn, A.M. (deposition date: 1992-05-01, release date: 1993-10-31, Last modification date: 2024-10-16)
Primary citationPowers, R.,Garrett, D.S.,March, C.J.,Frieden, E.A.,Gronenborn, A.M.,Clore, G.M.
Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy.
Science, 256:1673-1677, 1992
Cited by
PubMed Abstract: The three-dimensional solution structure of recombinant human interleukin-4, a protein of 133 residues and 15.4 kilodaltons that plays a key role in the immune and inflammatory systems, has been solved by multidimensional heteronuclear magnetic resonance spectroscopy. The structure is dominated by a left-handed four-helix bundle with an unusual topology comprising two overhand connections. The linker elements between the helices are formed by either long loops, small helical turns, or short strands. The overall topology is remarkably similar to that of growth hormone and granulocyte-macrophage colony stimulating factor, despite the absence of any sequence homology, and substantial differences in the relative lengths of the helices, the length and nature of the various connecting elements, and the pattern of disulfide bridges. These three proteins, however, bind to cell surface receptors belonging to the same hematopoietic superfamily, which suggests that interleukin-4 may interact with its receptor in an analogous manner to that observed in the crystal structure of the growth hormone-extracellular receptor complex.
PubMed: 1609277
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227111

數據於2024-11-06公開中

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