2HGF

HAIRPIN LOOP CONTAINING DOMAIN OF HEPATOCYTE GROWTH FACTOR, NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 2HGF

• Entry DOI: 10.2210/pdb2hgf/pdb
• Descriptor: HEPATOCYTE GROWTH FACTOR (1 entity in total)
• Functional Keywords: hepatocyte growth factor, scatter factor, hairpin loop, heparin binding, plasminogen related, nk1
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 11401.29

Authors

Zhou, H.,Mazzulla, M.J.,Kaufman, J.D.,Stahl, S.J.,Wingfield, P.T.,Rubin, J.S.,Bottaro, D.P.,Byrd, R.A. (deposition date: 1997-12-18, release date: 1998-06-24, Last modification date: 2024-10-23)

Primary citation

Zhou, H.,Mazzulla, M.J.,Kaufman, J.D.,Stahl, S.J.,Wingfield, P.T.,Rubin, J.S.,Bottaro, D.P.,Byrd, R.A.
The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site.
Structure, 6:109-116, 1998

PubMed Abstract: Hepatocyte growth factor (HGF) is a multipotent growth factor that transduces a wide range of biological signals, including mitogenesis, motogenesis, and morphogenesis. The N-terminal (N) domain of HGF, containing a hairpin-loop region, is important for receptor binding and the potent biological activities of HGF. The N domain is also the primary binding site for heparin or heparan sulfate, which enhances, receptor/ligand oligomerization and modulates receptor-dependent mitogenesis. The rational design of artificial modulators of HGF signaling requires a detailed understanding of the structures of HGF and its receptor, as well as the role of heparin proteoglycan; this study represents the first step towards that goal.

PubMed: 9493272
DOI: 10.1016/S0969-2126(98)00012-4

Experimental method

SOLUTION NMR