1ol0
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ol0 |SIZE=350|CAPTION= <scene name='initialview01'>1ol0</scene>, resolution 1.80Å | |PDB= 1ol0 |SIZE=350|CAPTION= <scene name='initialview01'>1ol0</scene>, resolution 1.80Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ol0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ol0 OCA], [http://www.ebi.ac.uk/pdbsum/1ol0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ol0 RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Vaughan, C K.]] | [[Category: Vaughan, C K.]] | ||
[[Category: Walsh, M A.]] | [[Category: Walsh, M A.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SO4]] | ||
[[Category: camelised variable heavy domain]] | [[Category: camelised variable heavy domain]] | ||
[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:46:52 2008'' |
Revision as of 19:46, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A CAMELISED HUMAN VH
Overview
The variable domain of dromedary immunoglobulins comprises only the heavy chain and is missing the light-chain variable domain. This single domain is sufficient for antigen recognition and binding-half that required by other mammals. Human antibody-VHs have previously been camelized to be soluble stable fragments that retain antigen binding. Such engineered VHH are of interest in drug development, since they are nonimmunogenic, and in other biotechnology applications. We present the structure of a camelized human antibody fragment (cVH), which is a competitive and reversible inhibitor of the NS3 serine protease of the hepatitis C virus (HCV). In solution, this cVH undergoes a concentration-dependent monomer-dimer equilibrium. The structure confirms the minimum mutational requirements of the VL-binding face. The fragment also suggests a means by which the observed dimerization occurs, highlighting the importance of the composition of the CDR3 in maintaining a truly camelized VH.
About this Structure
1OL0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a human VH: requirements for maintaining a monomeric fragment., Dottorini T, Vaughan CK, Walsh MA, LoSurdo P, Sollazzo M, Biochemistry. 2004 Jan 27;43(3):622-8. PMID:14730966
Page seeded by OCA on Sun Mar 30 22:46:52 2008
