1fcg: Difference between revisions

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New page: left|200px<br /> <applet load="1fcg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fcg, resolution 2.0Å" /> '''ECTODOMAIN OF HUMAN ...
 
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[[Image:1fcg.gif|left|200px]]<br />
[[Image:1fcg.gif|left|200px]]<br /><applet load="1fcg" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1fcg" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1fcg, resolution 2.0&Aring;" />
caption="1fcg, resolution 2.0&Aring;" />
'''ECTODOMAIN OF HUMAN FC GAMMA RECEPTOR, FCGRIIA'''<br />
'''ECTODOMAIN OF HUMAN FC GAMMA RECEPTOR, FCGRIIA'''<br />


==Overview==
==Overview==
Fc gamma receptors bind IgG to initiate cellular responses against, pathogens and soluble antigens. We have determined the three-dimensional, structure of the extracellular portion of human Fc gammaRIIa to 2.0 A, resolution providing a structural basis for the unique functions of the, leukocyte FcR family. The receptor is composed of two immunoglobulin, domains and arranged to expose the ligand-binding site at one end of, domain 2. Using alanine mutants we find that the binding sites for IgG1, and 2 are similar but the relative importance of specific regions on the, receptor varies. In crystals, Fc gammaRIIa molecules associate to resemble, V(L)V(H) dimers, suggesting that two Fc gammaRIIa molecules could, cooperate to bind IgG in an asymmetric manner.
Fc gamma receptors bind IgG to initiate cellular responses against pathogens and soluble antigens. We have determined the three-dimensional structure of the extracellular portion of human Fc gammaRIIa to 2.0 A resolution providing a structural basis for the unique functions of the leukocyte FcR family. The receptor is composed of two immunoglobulin domains and arranged to expose the ligand-binding site at one end of domain 2. Using alanine mutants we find that the binding sites for IgG1 and 2 are similar but the relative importance of specific regions on the receptor varies. In crystals, Fc gammaRIIa molecules associate to resemble V(L)V(H) dimers, suggesting that two Fc gammaRIIa molecules could cooperate to bind IgG in an asymmetric manner.


==Disease==
==Disease==
Known diseases associated with this structure: Lupus nephritis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=146790 146790]]
Known diseases associated with this structure: Lupus nephritis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=146790 146790]], Malaria, resistance to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604590 604590]], Systemic lupus erythematosus, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604590 604590]]


==About this Structure==
==About this Structure==
1FCG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1FCG OCA].  
1FCG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1FCG OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Garrett, T.P.]]
[[Category: Garrett, T P.]]
[[Category: Hogarth, P.M.]]
[[Category: Hogarth, P M.]]
[[Category: Maxwell, K.F.]]
[[Category: Maxwell, K F.]]
[[Category: Powell, M.S.]]
[[Category: Powell, M S.]]
[[Category: cd32]]
[[Category: cd32]]
[[Category: fc receptor]]
[[Category: fc receptor]]
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[[Category: leukocyte]]
[[Category: leukocyte]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:51:27 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:15 2008''