1rmf: Difference between revisions
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rm/1rmf_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rm/1rmf_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rmf ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rmf ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
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== Publication Abstract from PubMed == | |||
The specific binding of the monoclonal murine anti-intercellular adhesion molecule-1 (anti-ICAM-1) antibody, R6.5, inhibits the attachment of neutrophils to endothelium and prevents the attachment of major group human rhinovirus (HRV) to ICAM-1. This binding interferes with the host immune system and, as a result, the R6.5 antibody has been developed as a therapeutic anti-inflammatory and perhaps anti-HRV agent. The variable-region amino-acid sequence of R6.5 was determined from the anti-ICAM-1 cDNA. The crystallization conditions of the Fab fragment of R6.5 were established and the three-dimensional structure was determined by X-ray crystallography. The crystal space group is orthorhombic P2(1)2(1)2(1), a = 40.36, b = 137.76, c = 91.32 A, and the highest resolution of recorded reflections is 2.7 A. The molecular-replacement method using known Fab structures was employed to solve the R6.5 Fab structure. The final R-factor is 18.8% for a total of 3320 non-H protein atoms, 39 water molecules and 10 606 unique reflections. The protein exhibits the typical immunoglobulin fold. The surface contour of the antigen-combining site of the R6.5 antibody has a wide groove which resembles more the structure of an anti-polypeptide antibody than the structure of an anti-protein antibody. | |||
Structure of a monoclonal anti-ICAM-1 antibody R6.5 Fab fragment at 2.8 A resolution.,Jedrzejas MJ, Miglietta J, Griffin JA, Luo M Acta Crystallogr D Biol Crystallogr. 1995 May 1;51(Pt 3):380-5. PMID:15299305<ref>PMID:15299305</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 1rmf" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||