1fh5: Difference between revisions

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[[Image:1fh5.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_1fh5|  PDB=1fh5  |  SCENE=  }}  
{{STRUCTURE_1fh5|  PDB=1fh5  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF THE MONOCLONAL ANTIBODY MAK33'''
===CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF THE MONOCLONAL ANTIBODY MAK33===




==Overview==
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The Fab fragment of the murine monoclonal antibody, MAK33, directed against human creatine kinase of the muscle-type, was crystallized and the three-dimensional structure was determined to 2.9 A. The antigen-binding surface of MAK33 shows a convex overall shape typical for immunoglobulins binding large antigens. The structure allows us to analyze the environment of cis-prolyl-peptide bonds whose isomerization is of key importance in the folding process. These residues seem to be involved with not only domain stability but also seem to play a role in the association of heavy and light chains, reinforcing the importance of beta-strand recognition in antibody assembly. The structure also allows the localization of segments of primary sequence postulated to represent binding sites for the ER-specific chaperone BiP within the context of the entire Fab fragment. These sequences are found primarily in beta-strands that are necessary for interactions between the individual domains.
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{{ABSTRACT_PUBMED_11036070}}


==About this Structure==
==About this Structure==
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[[Category: Crystal structure]]
[[Category: Crystal structure]]
[[Category: Fab]]
[[Category: Fab]]
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