1ad0: Difference between revisions

Revision as of 12:43, 21 February 2008

FAB FRAGMENT OF ENGINEERED HUMAN MONOCLONAL ANTIBODY A5B7

OverviewOverview

The crystal structures of two pairs of Fab fragments have been determined. The pairs comprise both a murine and an engineered human form, each derived from the antitumor antibodies A5B7 and CTM01. Although antigen specificity is maintained within the pairs, antigen affinity varies. A comparison of the hypervariable loops for each pair of antibodies shows their structure has been well maintained in grafting, supporting the canonical loop model. Detailed structural analysis of the binding sites and domain arrangements for these antibodies suggests the differences in antigen affinity observed are likely to be due to inherent flexibility of the hypervariable loops and movements at the VL:VH domain interface. The four structures provide the first opportunity to study in detail the effects of protein engineering on specific antibodies.

About this StructureAbout this Structure

1AD0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

VL:VH domain rotations in engineered antibodies: crystal structures of the Fab fragments from two murine antitumor antibodies and their engineered human constructs., Banfield MJ, King DJ, Mountain A, Brady RL, Proteins. 1997 Oct;29(2):161-71. PMID:9329081

Page seeded by OCA on Thu Feb 21 11:43:12 2008

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OCA

@@ Line 4: / Line 4: @@
 ==Overview==
-The crystal structures of two pairs of Fab fragments have been determined., The pairs comprise both a murine and an engineered human form, each, derived from the antitumor antibodies A5B7 and CTM01. Although antigen, specificity is maintained within the pairs, antigen affinity varies. A, comparison of the hypervariable loops for each pair of antibodies shows, their structure has been well maintained in grafting, supporting the, canonical loop model. Detailed structural analysis of the binding sites, and domain arrangements for these antibodies suggests the differences in, antigen affinity observed are likely to be due to inherent flexibility of, the hypervariable loops and movements at the VL:VH domain interface. The, four structures provide the first opportunity to study in detail the, effects of protein engineering on specific antibodies.
+The crystal structures of two pairs of Fab fragments have been determined. The pairs comprise both a murine and an engineered human form, each derived from the antitumor antibodies A5B7 and CTM01. Although antigen specificity is maintained within the pairs, antigen affinity varies. A comparison of the hypervariable loops for each pair of antibodies shows their structure has been well maintained in grafting, supporting the canonical loop model. Detailed structural analysis of the binding sites and domain arrangements for these antibodies suggests the differences in antigen affinity observed are likely to be due to inherent flexibility of the hypervariable loops and movements at the VL:VH domain interface. The four structures provide the first opportunity to study in detail the effects of protein engineering on specific antibodies.
 ==About this Structure==
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 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Banfield, M.J.]]
+[[Category: Banfield, M J.]]
-[[Category: Brady, R.L.]]
+[[Category: Brady, R L.]]
 [[Category: fab fragment]]
 [[Category: immunoglobulin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:28:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:12 2008''