Global structure of HIV-1 neutralizing antibody IgG1 b12 is asymmetric.
IR@IMTECH: CSIR-Institute of Microbial Technology, Chandigarh
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| Title |
Global structure of HIV-1 neutralizing antibody IgG1 b12 is asymmetric.
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| Creator |
Ganguly, Ashish
Solanki, Ashish K Boone, Christopher D Krueger, Joanna K |
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| Subject |
QD Chemistry
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| Description |
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.
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| Publisher |
Elsevier Science
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| Date |
2010-01-01
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| Type |
Article
PeerReviewed |
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| Relation |
http://www.sciencedirect.com/science/article/pii/S0006291X09023663
http://crdd.osdd.net/open/541/ |
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| Identifier |
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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