1him: Difference between revisions
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[[Image:1him.gif|left|200px]] | [[Image:1him.gif|left|200px]] | ||
'''STRUCTURAL EVIDENCE FOR INDUCED FIT AS A MECHANISM FOR ANTIBODY-ANTIGEN RECOGNITION''' | {{Structure | ||
|PDB= 1him |SIZE=350|CAPTION= <scene name='initialview01'>1him</scene>, resolution 2.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURAL EVIDENCE FOR INDUCED FIT AS A MECHANISM FOR ANTIBODY-ANTIGEN RECOGNITION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HIM is a [ | 1HIM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HIM OCA]. | ||
==Reference== | ==Reference== | ||
Structural evidence for induced fit as a mechanism for antibody-antigen recognition., Rini JM, Schulze-Gahmen U, Wilson IA, Science. 1992 Feb 21;255(5047):959-65. PMID:[http:// | Structural evidence for induced fit as a mechanism for antibody-antigen recognition., Rini JM, Schulze-Gahmen U, Wilson IA, Science. 1992 Feb 21;255(5047):959-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1546293 1546293] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Schulze-Gahmen, U.]] | [[Category: Schulze-Gahmen, U.]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:37:33 2008'' |
Revision as of 12:37, 20 March 2008
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, resolution 2.9Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
STRUCTURAL EVIDENCE FOR INDUCED FIT AS A MECHANISM FOR ANTIBODY-ANTIGEN RECOGNITION
OverviewOverview
The three-dimensional structure of a specific antibody (Fab 17/9) to a peptide immunogen from influenza virus hemagglutinin [HA1(75-110)] and two independent crystal complexes of this antibody with bound peptide (TyrP100-LeuP108) have been determined by x-ray crystallographic techniques at 2.0 A, 2.9 A, and 3.1 A resolution, respectively. The nonapeptide antigen assumes a type I beta turn in the antibody combining site and interacts primarily with the Fab hypervariable loops L3, H2, and H3. Comparison of the bound and unbound Fab structures shows that a major rearrangement in the H3 loop accompanies antigen binding. This conformational change results in the creation of a binding pocket for the beta turn of the peptide, allowing TyrP105 to be accommodated. The conformation of the peptide bound to the antibody shows similarity to its cognate sequence in the HA1, suggesting a possible mechanism for the cross-reactivity of this Fab with monomeric hemagglutinin. The structures of the free and antigen bound antibodies demonstrate the flexibility of the antibody combining site and provide an example of induced fit as a mechanism for antibody-antigen recognition.
About this StructureAbout this Structure
1HIM is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Structural evidence for induced fit as a mechanism for antibody-antigen recognition., Rini JM, Schulze-Gahmen U, Wilson IA, Science. 1992 Feb 21;255(5047):959-65. PMID:1546293
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