1dn2
From Proteopedia
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| - | [[Image:1dn2.gif|left|200px]] | + | [[Image:1dn2.gif|left|200px]] |
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| - | '''FC FRAGMENT OF HUMAN IGG1 IN COMPLEX WITH AN ENGINEERED 13 RESIDUE PEPTIDE DCAWHLGELVWCT-NH2''' | + | {{Structure |
| + | |PDB= 1dn2 |SIZE=350|CAPTION= <scene name='initialview01'>1dn2</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''FC FRAGMENT OF HUMAN IGG1 IN COMPLEX WITH AN ENGINEERED 13 RESIDUE PEPTIDE DCAWHLGELVWCT-NH2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DN2 is a [ | + | 1DN2 is a [[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=1DN2 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10678837 10678837] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: fc igg phage display peptide]] | [[Category: fc igg phage display peptide]] | ||
| - | ''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 10:41:05 2008'' |
Revision as of 08:41, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 10:41:05 2008
