1ol0

Crystal structure of a camelised human VH

spinqualitylabelsall models 1ol0, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ol0 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: GOL, MSE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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