1ol0: Difference between revisions

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[[Image:1ol0.gif|left|200px]]
{{Seed}}
[[Image:1ol0.png|left|200px]]


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{{STRUCTURE_1ol0|  PDB=1ol0  |  SCENE=  }}  
{{STRUCTURE_1ol0|  PDB=1ol0  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF A CAMELISED HUMAN VH'''
===CRYSTAL STRUCTURE OF A CAMELISED HUMAN VH===




==Overview==
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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.
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{{ABSTRACT_PUBMED_14730966}}


==About this Structure==
==About this Structure==
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[[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 Sat May  3 03:59:24 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:53:55 2008''

Revision as of 01:54, 28 July 2008

File:1ol0.png

Template:STRUCTURE 1ol0

CRYSTAL STRUCTURE OF A CAMELISED HUMAN VH

Template:ABSTRACT PUBMED 14730966

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

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