1H0D

Crystal structure of Human Angiogenin in complex with Fab fragment of its monoclonal antibody mAb 26-2F

Summary for 1H0D

• Entry DOI: 10.2210/pdb1h0d/pdb
• Descriptor: ANTIBODY FAB FRAGMENT, LIGHT CHAIN, ANTIBODY FAB FRAGMENT, HEAVY CHAIN, ANGIOGENIN, ... (6 entities in total)
• Functional Keywords: immune system/hydrolase, complex (antibody-hydrolase), ribonuclease, antibody, immune system-hydrolase complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 3
• Total formula weight: 62715.74

Authors

Chavali, G.B.,Papageorgiou, A.C.,Acharya, K.R. (deposition date: 2002-06-19, release date: 2003-06-19, Last modification date: 2024-11-13)

Primary citation

Chavali, G.B.,Papageorgiou, A.C.,Olson, K.,Fett, J.,Hu, G.,Shapiro, R.,Acharya, K.R.
The Crystal Structure of Human Angiogenin in Complex with an Antitumor Neutralizing Antibody
Structure, 11:875-, 2003

PubMed Abstract: The murine monoclonal antibody 26-2F neutralizes the angiogenic and ribonucleolytic activities of human angiogenin (ANG) and is highly effective in preventing the establishment and metastatic dissemination of human tumors in athymic mice. Here we report a 2.0 A resolution crystal structure for the complex of ANG with the Fab fragment of 26-2F that reveals the detailed interactions between ANG and the complementarity-determining regions (CDRs) of the antibody. Surprisingly, Fab binding induces a dramatic conformational change in the cell binding region of ANG at the opposite end of the molecule from the combining site; crosslinking experiments indicate that this rearrangement also occurs in solution. The ANG-Fab complex structure should be invaluable for designing maximally humanized versions of 26-2F for potential clinical use.

PubMed: 12842050
DOI: 10.1016/S0969-2126(03)00131-X

Experimental method

X-RAY DIFFRACTION (2 Å)