1rvf
From Proteopedia
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- | [[Image:1rvf.jpg|left|200px]] | + | [[Image:1rvf.jpg|left|200px]] |
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- | '''FAB COMPLEXED WITH INTACT HUMAN RHINOVIRUS''' | + | {{Structure |
+ | |PDB= 1rvf |SIZE=350|CAPTION= <scene name='initialview01'>1rvf</scene>, resolution 4.0Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''FAB COMPLEXED WITH INTACT HUMAN RHINOVIRUS''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1RVF is a [ | + | 1RVF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Human_rhinovirus_10 Human rhinovirus 10], [http://en.wikipedia.org/wiki/Human_rhinovirus_sp. Human rhinovirus sp.] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The following page contains interesting information on the relation of 1RVF with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb20_1.html Poliovirus and Rhinovirus]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RVF OCA]. |
==Reference== | ==Reference== | ||
- | Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon., Smith TJ, Chase ES, Schmidt TJ, Olson NH, Baker TS, Nature. 1996 Sep 26;383(6598):350-4. PMID:[http:// | + | Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon., Smith TJ, Chase ES, Schmidt TJ, Olson NH, Baker TS, Nature. 1996 Sep 26;383(6598):350-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8848050 8848050] |
[[Category: Human rhinovirus 10]] | [[Category: Human rhinovirus 10]] | ||
[[Category: Human rhinovirus sp.]] | [[Category: Human rhinovirus sp.]] | ||
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[[Category: thiol protease]] | [[Category: thiol protease]] | ||
- | ''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 13:56:46 2008'' |
Revision as of 11:56, 20 March 2008
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, resolution 4.0Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
FAB COMPLEXED WITH INTACT HUMAN RHINOVIRUS
Overview
The three-dimensional structure of intact human rhinovirus 14 (HRV-14) complexed with Fab fragments (Fab17-IA) from a strongly neutralizing antibody that binds bivalently to the virion has been determined to 4.0 angstrom resolution by a combination of X-ray crystallography and cryo-electron microscopy. In contradiction to the most commonly held model of antibody-mediated neutralization, Fab17-IA does not induce a conformational change in the HRV-14 capsid. Instead, the paratope of the antibody undergoes a large conformational change to accommodate the epitope. Unlike any previously described antibody-antigen structure, the conserved framework region of the antibody makes extensive contact with the viral surface. Fab17-IA penetrates deep within the canyon in which the cellular receptor for HRV-14 binds. Hence, it is unlikely that viral quaternary structure evolves merely to evade immune recognition. Instead, the shape and position of the receptor-binding region on a virus probably dictates receptor binding and subsequent uncoating events and has little or no influence on concealing the virus from the immune system.
About this Structure
1RVF is a Protein complex structure of sequences from Human rhinovirus 10, Human rhinovirus sp. and Mus musculus. The following page contains interesting information on the relation of 1RVF with [Poliovirus and Rhinovirus]. Full crystallographic information is available from OCA.
Reference
Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon., Smith TJ, Chase ES, Schmidt TJ, Olson NH, Baker TS, Nature. 1996 Sep 26;383(6598):350-4. PMID:8848050
Page seeded by OCA on Thu Mar 20 13:56:46 2008
Categories: Human rhinovirus 10 | Human rhinovirus sp. | Mus musculus | Poliovirus and Rhinovirus | Protein complex | Smith, T J. | Coat protein | Complex (coat protein/immunoglobulin) | Core protein | Hydrolase | Icosahedral virus | Myristylation | Polyprotein | Rna-directed rna polymerase | Thiol protease