|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0078058,
umls-concept:C0378516,
umls-concept:C0439855,
umls-concept:C0444626,
umls-concept:C0597357,
umls-concept:C1256770,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2699488
|
|
pubmed:issue |
5
|
|
pubmed:dateCreated |
1997-12-29
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Vascular endothelial growth factor (VEGF) is a homodimeric hormone that induces proliferation of endothelial cells through binding to the kinase domain receptor and the Fms-like tyrosine kinase receptor (Flt-1), the extracellular portions of which consist of seven immunoglobulin domains. We show that the second and third domains of Flt-1 are necessary and sufficient for binding VEGF with near-native affinity, and that domain 2 alone binds only 60-fold less tightly than wild-type. The crystal structure of the complex between VEGF and the second domain of Flt-1 shows domain 2 in a predominantly hydrophobic interaction with the "poles" of the VEGF dimer. Based on this structure and on mutational data, we present a model of VEGF bound to the first four domains of Flt-1.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
0092-8674
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
28
|
|
pubmed:volume |
91
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
695-704
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:9393862-Cells, Cultured,
pubmed-meshheading:9393862-Crystallography,
pubmed-meshheading:9393862-Endothelial Growth Factors,
pubmed-meshheading:9393862-Lymphokines,
pubmed-meshheading:9393862-Molecular Sequence Data,
pubmed-meshheading:9393862-Mutagenesis,
pubmed-meshheading:9393862-Peptide Fragments,
pubmed-meshheading:9393862-Protein Binding,
pubmed-meshheading:9393862-Protein Structure, Secondary,
pubmed-meshheading:9393862-Protein Structure, Tertiary,
pubmed-meshheading:9393862-Proto-Oncogene Proteins,
pubmed-meshheading:9393862-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:9393862-Receptors, Platelet-Derived Growth Factor,
pubmed-meshheading:9393862-Sequence Homology, Amino Acid,
pubmed-meshheading:9393862-Vascular Endothelial Growth Factor A,
pubmed-meshheading:9393862-Vascular Endothelial Growth Factor Receptor-1,
pubmed-meshheading:9393862-Vascular Endothelial Growth Factors
|
|
pubmed:year |
1997
|
|
pubmed:articleTitle |
Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor.
|
|
pubmed:affiliation |
Genentech, Inc., Department of Protein Engineering, South San Francisco, California 94080, USA.
|
|
pubmed:publicationType |
Journal Article
|
