Structural highlights
Function
IGH1M_MOUSE
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 three-dimensional structure of the antigen-binding fragment of a monoclonal antibody to human interleukin-2 in a new crystal form (space group P2(1)2(1)2(1); unit cell parameters: a = 42.82, b = 90.68, and c = 139.82 A) was determined by the X-ray molecular replacement method at the resolution of 2.7 A. The protein folding and the stereochemistry of its antigen-binding site were comparatively analyzed. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2004, vol. 30, no. 5; see also http: // www.maik.ru.
[A new crystal form of the Fab fragment of a monoclonal antibody to human interleukin-2: the three-dimensional structure at 2.7 A resolution].,Pletnev VZ, Goriacheva EA, Tsygannik IN, Nesmeianov VA, Pletnev SV, Pangborn W, Daux W Bioorg Khim. 2004 Sep-Oct;30(5):466-9. PMID:15562966[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pletnev VZ, Goriacheva EA, Tsygannik IN, Nesmeianov VA, Pletnev SV, Pangborn W, Daux W. [A new crystal form of the Fab fragment of a monoclonal antibody to human interleukin-2: the three-dimensional structure at 2.7 A resolution]. Bioorg Khim. 2004 Sep-Oct;30(5):466-9. PMID:15562966
