1wbr
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1wbr |SIZE=350|CAPTION= <scene name='initialview01'>1wbr</scene> | |PDB= 1wbr |SIZE=350|CAPTION= <scene name='initialview01'>1wbr</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wbr OCA], [http://www.ebi.ac.uk/pdbsum/1wbr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wbr RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Roesch, P.]] | [[Category: Roesch, P.]] | ||
[[Category: Willbold, D.]] | [[Category: Willbold, D.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: NH2]] | ||
[[Category: cd4(403-419) receptor peptide]] | [[Category: cd4(403-419) receptor peptide]] | ||
[[Category: hiv]] | [[Category: hiv]] | ||
| Line 32: | Line 33: | ||
[[Category: vpu]] | [[Category: vpu]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:34:04 2008'' |
Revision as of 21:34, 30 March 2008
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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