1wbr
From Proteopedia
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| - | [[Image:1wbr.jpg|left|200px]] | + | [[Image:1wbr.jpg|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF THE HUMAN CD4 (403-419) RECEPTOR PEPTIDE, NMR, 32 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1wbr |SIZE=350|CAPTION= <scene name='initialview01'>1wbr</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF THE HUMAN CD4 (403-419) RECEPTOR PEPTIDE, NMR, 32 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
The cytoplasmic part of CD4 is known to be essential for the interaction with the human immunodeficiency virus type 1 proteins Vpu and Nef. The 17 amino acid synthetic peptide CD4 (403-419) with the amino acid sequence of the membrane proximal part of the cytoplasmic domain of the human CD4 receptor was structurally investigated by circular dichroism and nuclear magnetic resonance spectroscopy. The average alpha-helical content of the peptide could be estimated to be around 25%. Chemical shift index analysis and the connectivity pattern in nuclear Overhauser enhancement spectra located the alpha-helical part of the peptide from Gln403 to Arg412. It may be speculated that this amphipathic alpha-helix is the contact region with the Vpu and Nef proteins. Copyright 1996 S. Karger AG, Basel | The cytoplasmic part of CD4 is known to be essential for the interaction with the human immunodeficiency virus type 1 proteins Vpu and Nef. The 17 amino acid synthetic peptide CD4 (403-419) with the amino acid sequence of the membrane proximal part of the cytoplasmic domain of the human CD4 receptor was structurally investigated by circular dichroism and nuclear magnetic resonance spectroscopy. The average alpha-helical content of the peptide could be estimated to be around 25%. Chemical shift index analysis and the connectivity pattern in nuclear Overhauser enhancement spectra located the alpha-helical part of the peptide from Gln403 to Arg412. It may be speculated that this amphipathic alpha-helix is the contact region with the Vpu and Nef proteins. Copyright 1996 S. Karger AG, Basel | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: CD4 lymphocyte deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=186940 186940]], Lupus erythematosus, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=186940 186940]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 1WBR is a [ | + | 1WBR 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=1WBR OCA]. |
==Reference== | ==Reference== | ||
| - | Solution Structure of the Human CD4 (403-419) Receptor Peptide., Willbold D, Rosch P, J Biomed Sci. 1996 Nov;3(6):435-441. PMID:[http:// | + | Solution Structure of the Human CD4 (403-419) Receptor Peptide., Willbold D, Rosch P, J Biomed Sci. 1996 Nov;3(6):435-441. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11725124 11725124] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: vpu]] | [[Category: vpu]] | ||
| - | ''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 14:54:54 2008'' |
Revision as of 12:54, 20 March 2008
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE HUMAN CD4 (403-419) RECEPTOR PEPTIDE, NMR, 32 STRUCTURES
Overview
The cytoplasmic part of CD4 is known to be essential for the interaction with the human immunodeficiency virus type 1 proteins Vpu and Nef. The 17 amino acid synthetic peptide CD4 (403-419) with the amino acid sequence of the membrane proximal part of the cytoplasmic domain of the human CD4 receptor was structurally investigated by circular dichroism and nuclear magnetic resonance spectroscopy. The average alpha-helical content of the peptide could be estimated to be around 25%. Chemical shift index analysis and the connectivity pattern in nuclear Overhauser enhancement spectra located the alpha-helical part of the peptide from Gln403 to Arg412. It may be speculated that this amphipathic alpha-helix is the contact region with the Vpu and Nef proteins. Copyright 1996 S. Karger AG, Basel
About this Structure
1WBR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution Structure of the Human CD4 (403-419) Receptor Peptide., Willbold D, Rosch P, J Biomed Sci. 1996 Nov;3(6):435-441. PMID:11725124
Page seeded by OCA on Thu Mar 20 14:54:54 2008
Categories: Homo sapiens | Single protein | Roesch, P. | Willbold, D. | ACE | NH2 | Cd4(403-419) receptor peptide | Hiv | Immunoglobulin fold | Nmr | Vpu
