1fh5: Difference between revisions

Revision as of 13:38, 21 February 2008

CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF THE MONOCLONAL ANTIBODY MAK33

OverviewOverview

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.

About this StructureAbout this Structure

1FH5 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone bip., Augustine JG, de La Calle A, Knarr G, Buchner J, Frederick CA, J Biol Chem. 2001 Feb 2;276(5):3287-94. Epub 2000 Oct 17. PMID:11036070

Page seeded by OCA on Thu Feb 21 12:38:36 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1fh5.gif|left|200px]]<br />
+[[Image:1fh5.gif|left|200px]]<br /><applet load="1fh5" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1fh5" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1fh5, resolution 2.9&Aring;" />
 '''CRYSTAL STRUCTURE OF THE FAB FRAGMENT OF THE MONOCLONAL ANTIBODY MAK33'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-FH5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FH5 OCA].
+FH5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FH5 OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Augustine, J.G.]]
+[[Category: Augustine, J G.]]
 [[Category: Buchner, J.]]
-[[Category: Calle, A.de.la.]]
+[[Category: Calle, A de la.]]
-[[Category: Frederick, C.A.]]
+[[Category: Frederick, C A.]]
 [[Category: Knarr, G.]]
 [[Category: bip]]
@@ Line 23: / Line 22: @@
 [[Category: fab]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:30:12 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:36 2008''