Global structure of HIV-1 neutralizing antibody IgG1 b12 is asymmetric.

Ganguly, Ashish and Solanki, Ashish K and Boone, Christopher D and Krueger, Joanna K (2010) Global structure of HIV-1 neutralizing antibody IgG1 b12 is asymmetric. Biochemical and biophysical research communications, 391 (1). pp. 947-51. ISSN 1090-2104

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Human antibody IgG1 b12 is one of the four antibodies known to neutralize a broad range of human immunodeficiency virus-1. The crystal structure of this antibody displayed an asymmetric disposition of the Fab arms relative to its Fc portion. Comparison of structures solved for other IgG1 antibodies led to a notion that crystal packing forces entrapped a "snap-shot" of different conformations accessible to this antibody. To elucidate global structure of this unique antibody, we acquired small-angle X-ray scattering data from its dilute solution. Data analysis indicated that b12 adopts a bilobal globular structure in solution with a radius of gyration and a maximum linear dimension of approximately 54 and approximately 180A, respectively. Extreme similarity between its solution and crystal structure concludes that non-flexible, asymmetric shape is an inherent property of this rare antibody.

Item Type: Article
Additional Information: Copyright of this article belongs to Elsevier Science
Uncontrolled Keywords: HIV-1 neutralizing antibody; Small-angle X-ray scattering; Molecular modeling; Guinier approximation; Kratky analysis
Subjects: Q Science > QD Chemistry
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 08 Dec 2011 19:32
Last Modified: 22 Jul 2015 03:56

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