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1ITM

ANALYSIS OF THE SOLUTION STRUCTURE OF HUMAN INTERLEUKIN 4 DETERMINED BY HETERONUCLEAR THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE TECHNIQUES

Summary for 1ITM
Entry DOI10.2210/pdb1itm/pdb
DescriptorINTERLEUKIN-4 (1 entity in total)
Functional Keywordscytokine
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P05112
Total number of polymer chains1
Total formula weight15120.44
Authors
Redfield, C.,Smith, L.J.,Boyd, J.,Lawrence, G.M.P.,Edwards, R.G.,Gershater, C.J.,Smith, R.A.G.,Dobson, C.M. (deposition date: 1994-02-28, release date: 1994-05-31, Last modification date: 2024-11-20)
Primary citationRedfield, C.,Smith, L.J.,Boyd, J.,Lawrence, G.M.,Edwards, R.G.,Gershater, C.J.,Smith, R.A.,Dobson, C.M.
Analysis of the solution structure of human interleukin-4 determined by heteronuclear three-dimensional nuclear magnetic resonance techniques.
J.Mol.Biol., 238:23-41, 1994
Cited by
PubMed Abstract: Human interleukin-4 (IL-4) is a member of the family of haemopoietic cytokines that modulate cell proliferation and differentiation within the immune system. It has a four-helix-bundle structure, and possesses a high degree of mobility in certain regions, notably in the two long loops running the length of the bundle in its up-up-down-down topology. Information from a variety of three-dimensional heteronuclear NMR experiments, including chemical shifts, coupling constants and NOE data, is analysed in terms of the solution structure of IL-4. In addition, structure calculations with and without specific restraints such as hydrogen bond location or torsion angle restrictions are compared in the light of the dynamic behaviour of the polypeptide chain. Particular emphasis is placed on defining the lengths and positions of secondary structure elements, and on the likely structural preferences within the less well ordered loop regions. The overall topology of IL-4 is compared with those defined in recent structure determinations of related proteins. This analysis is combined with recent mutagenesis data to propose a possible mode of interaction of IL-4 with its receptor.
PubMed: 8145254
DOI: 10.1006/jmbi.1994.1265
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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