Motion in Human Interluekin 5 [hil5]

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Classification Known Domain Motion, Shear Mechanism [D-s-2]

Verschelde et al. report that human interleuking 5 (hIL5) can assume at least two distinct conformations. Specifically, the NH2 terminal helix A shifts approximately 2A, while the loop between helix B and C take on different conformations. The C-terminal helix D shows a smaller shift of 1A. They clearly observe a global deformation of the dimer when the two conformations are compared. This motion causes a narrowing or broadening of the cleft between the monomers. Both monomers appear to rotate around an axis causing this global deformation. Helix pairs A,D and B,C form a layered architecture, with one layer sliding over the other. This pair of helices are crossed, the prefered geometry for shearing before of the small interface between the two layers. They classify the motion as a shear mechanism resulting in domain rotation.

Particular values describing motion
Creation Date = 19971130
Experimental Methods = x (Traditional x-ray)
Modification Date = 1999-07-27 14:02:56.000

J-L Verschelde, C Ampe, Y Guisez, C Oefner, J Vandekerckhove, J Tavernier (1998). Analysis of three human interleukin 5 structures reveals a possible receptor binding mechanism. FEBS Lett 1998 Mar 13;424(3):121-6 [Medline info for 9539134]

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