1dn2
From Proteopedia
(New page: 200px<br /> <applet load="1dn2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dn2, resolution 2.7Å" /> '''FC FRAGMENT OF HUMAN...) |
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| - | [[Image:1dn2.gif|left|200px]]<br /> | + | [[Image:1dn2.gif|left|200px]]<br /><applet load="1dn2" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1dn2" size=" | + | |
caption="1dn2, resolution 2.7Å" /> | caption="1dn2, resolution 2.7Å" /> | ||
'''FC FRAGMENT OF HUMAN IGG1 IN COMPLEX WITH AN ENGINEERED 13 RESIDUE PEPTIDE DCAWHLGELVWCT-NH2'''<br /> | '''FC FRAGMENT OF HUMAN IGG1 IN COMPLEX WITH AN ENGINEERED 13 RESIDUE PEPTIDE DCAWHLGELVWCT-NH2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The hinge region on the Fc fragment of human immunoglobulin G interacts | + | The hinge region on the Fc fragment of human immunoglobulin G interacts with at least four different natural protein scaffolds that bind at a common site between the C(H2) and C(H3) domains. This "consensus" site was also dominant for binding of random peptides selected in vitro for high affinity (dissociation constant, about 25 nanomolar) by bacteriophage display. Thus, this site appears to be preferred owing to its intrinsic physiochemical properties, and not for biological function alone. A 2.7 angstrom crystal structure of a selected 13-amino acid peptide in complex with Fc demonstrated that the peptide adopts a compact structure radically different from that of the other Fc binding proteins. Nevertheless, the specific Fc binding interactions of the peptide strongly mimic those of the other proteins. Juxtaposition of the available Fc-complex crystal structures showed that the convergent binding surface is highly accessible, adaptive, and hydrophobic and contains relatively few sites for polar interactions. These are all properties that may promote cross-reactive binding, which is common to protein-protein interactions and especially hormone-receptor complexes. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1DN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DN2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: DeLano, W | + | [[Category: DeLano, W L.]] |
| - | [[Category: Ultsch, M | + | [[Category: Ultsch, M H.]] |
| - | [[Category: Vos, A | + | [[Category: Vos, A M.de.]] |
| - | [[Category: Wells, J | + | [[Category: Wells, J A.]] |
[[Category: NH2]] | [[Category: NH2]] | ||
[[Category: fc igg phage display peptide]] | [[Category: fc igg phage display peptide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:20 2008'' |
Revision as of 10:18, 21 February 2008
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FC FRAGMENT OF HUMAN IGG1 IN COMPLEX WITH AN ENGINEERED 13 RESIDUE PEPTIDE DCAWHLGELVWCT-NH2
Contents |
Overview
The hinge region on the Fc fragment of human immunoglobulin G interacts with at least four different natural protein scaffolds that bind at a common site between the C(H2) and C(H3) domains. This "consensus" site was also dominant for binding of random peptides selected in vitro for high affinity (dissociation constant, about 25 nanomolar) by bacteriophage display. Thus, this site appears to be preferred owing to its intrinsic physiochemical properties, and not for biological function alone. A 2.7 angstrom crystal structure of a selected 13-amino acid peptide in complex with Fc demonstrated that the peptide adopts a compact structure radically different from that of the other Fc binding proteins. Nevertheless, the specific Fc binding interactions of the peptide strongly mimic those of the other proteins. Juxtaposition of the available Fc-complex crystal structures showed that the convergent binding surface is highly accessible, adaptive, and hydrophobic and contains relatively few sites for polar interactions. These are all properties that may promote cross-reactive binding, which is common to protein-protein interactions and especially hormone-receptor complexes.
Disease
Known disease associated with this structure: Agammaglobulinemia OMIM:[147020]
About this Structure
1DN2 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Convergent solutions to binding at a protein-protein interface., DeLano WL, Ultsch MH, de Vos AM, Wells JA, Science. 2000 Feb 18;287(5456):1279-83. PMID:10678837
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