1BHT

NK1 FRAGMENT OF HUMAN HEPATOCYTE GROWTH FACTOR

Summary for 1BHT

• Entry DOI: 10.2210/pdb1bht/pdb
• Descriptor: HEPATOCYTE GROWTH FACTOR, SULFATE ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: heparin-binding domain, kringle, c-met receptor angonist/ antagonist, growth factor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 41383.39

Authors

Ultsch, M.H.,Lokker, N.A.,Godowski, P.J.,De Vos, A.M. (deposition date: 1998-06-10, release date: 1998-11-04, Last modification date: 2024-10-16)

Primary citation

Ultsch, M.,Lokker, N.A.,Godowski, P.J.,de Vos, A.M.
Crystal structure of the NK1 fragment of human hepatocyte growth factor at 2.0 A resolution.
Structure, 6:1383-1393, 1998

PubMed Abstract: Hepatocyte growth factor (HGF) is a mitogen for hepatocytes and has also been implicated as an epithelial morphogen in tumor invasion. HGF activates its specific cellular receptor, c-met, through an aggregation mechanism potentiated by heparan sulfate glycosaminoglycans. HGF consists of an N-terminal (N) domain, four kringle domains (the first of which carries receptor-binding determinants), and an inactive serine-protease-like domain. NK1, a naturally occurring fragment of HGF, acts as an antagonist of HGF in the absence of heparin.

PubMed: 9817840
DOI: 10.1016/S0969-2126(98)00138-5

Experimental method

X-RAY DIFFRACTION (2 Å)