NDLI: Modeling the alpha IIb beta 3 integrin solution conformation.

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Modeling the alpha IIb beta 3 integrin solution conformation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Rocco, M. Spotorno, B. Hantgan, R. R.
Description	Country affiliation: Italy Author Affiliation: Rocco M ( Biostructures Unit, Istituto Nazionale per la Ricerca sul Cancro, IST, Genova, Italy.)
Abstract	The alpha IIb beta 3 platelet integrin is the prototypical member of a widely distributed class of transmembrane receptors formed by the noncovalent association of alpha and beta subunits. Electron microscopic (EM) images of the alpha IIb beta 3 complex show an asymmetric particle with a globular domain from which two extended regions protrude to contact the lipid bilayer. Distance constraints provided by disulfide bond patterns, epitope mapping, and ligand mimetic cross-linking studies rather suggest a somewhat more compact conformation for the alpha IIb beta 3 complex. We have studied the shape of detergent-solubilized alpha IIb beta 3 by employing a low-resolution modeling procedure in which each polypeptide has been represented as an array of interconnected, nonoverlapping spheres (beads) of various sizes. The number, size, and three-dimensional relationships among the beads were defined either solely by dimensions obtained from published EM images of integrin receptors (EM models, 21 beads), or solely by interdomain constraints derived from published biochemical data (biochemical model, 37 beads). Interestingly, although no EM data were employed in its construction, the resulting overall shape of the biochemical model was still compatible with the EM data. Both kinds of models were then evaluated for their calculated solution properties. The more elongated EM models have diffusion and sedimentation coefficients that differ, at best, by +2% and -18% from the experimental values, determined, respectively, in octyl glucoside and Triton X-100. On the other hand, the parameters calculated for the more compact biochemical model showed a more consistent agreement with experimental values, differing by -7% (octyl glucoside) to -6% (Triton X-100). Thus, it appears that using the biochemical constraints as a starting point has resulted in not only a more detailed model of the detergent-solubilized alpha IIb beta 3 complex, where the relative spatial location of specific domains the size of 5-10 kDa can be tentatively mapped, but in a model that can also reconcile the electron microscopy with the biochemical and the solution data.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	12
Volume Number	2
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1993-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Integrins Chemistry Ultrastructure Protein Conformation Amino Acid Sequence Carbohydrate Sequence Computer Simulation Models, Chemical Models, Structural Molecular Sequence Data Platelet Glycoprotein Gpiib-iiia Complex Comparative Study Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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