Motion in Immunoglobulin (CDR motion) [igcdr]

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Classification Known Fragment Motion, Hinge Mechanism [F-h-2]

Structures 1GIG Bizebard et al. structure with HAHC19 Uncomplexed [ PartsList ] 1HIL 17/9 Conformation 1 [ PartsList ] 1HIM 17/9 Conformation 2 [ PartsList ] ???? Complex structure not in the databank on 13-Dec-95.HC19 Complexed

Description For 17/9, upon binding antigen the H3 loop in this antibody switches in a different conformation. This moves alpha carbons by up to 4.6 A and sidechains atoms by up to 9 A. For HC, upon binding antigen (HA) the H3 loop in this antibody switches to a different conformation. This moves sidechains atoms by up to 10 A. (from the paper). Heavy chain residues Y102 and D103 move the most.

Particular values describing motion Annotation Level (1..10) = 4 Maximum CA displacement (A) = 4.6 (For 17/9) Maximum atomic displacement (A) = 10 (For HC19) Maximum atomic displacement (A) = 9 (For 17/9) Experimental Methods = x (Traditional x-ray) Creation Date = 19970822 Modification Date = 19970822

References J M Rini, U Schulze-Gahmen and I A Wilson (1992). Structural Evidence for Induced-fit as a Mechanism for Antibody-antigen Recognition. Science. 255: 959-965. [Medline info for 92188158] J M Rini, U Schulze-Gahmen and I A Wilson (1992). Structural Evidence for Induced-fit as a Mechanism for Antibody-antigen Recognition. Science. 255: 959-965. [Medline info for 94087724] Bizebard T et al., Structure of influenza virus haemagglutinin complexed with a neutralizing antibody. Nature, 1995 Jul 6, 376(6535):92-4. [Medline info for 95319545]

Data and Graphics Graphic-1 General folding topology of the immunoglobulins. This shows the location of H3.

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu