1VR2
HUMAN VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 (KDR) KINASE DOMAIN
Summary for 1VR2
Entry DOI | 10.2210/pdb1vr2/pdb |
Descriptor | PROTEIN (VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR KINASE) (2 entities in total) |
Functional Keywords | tyrosine kinase, transferase |
Biological source | Homo sapiens (human) More |
Cellular location | Cell junction . Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted . Isoform 3: Secreted: P35968 |
Total number of polymer chains | 1 |
Total formula weight | 36274.74 |
Authors | Mctigue, M.,Wickersham, J.,Pinko, C.,Showalter, R.,Parast, C.,Tempczyk-Russell, A.,Gehring, M.,Mroczkowski, B.,Kan, C.,Villafranca, J.,Appelt, K. (deposition date: 1998-12-03, release date: 2000-03-15, Last modification date: 2023-11-15) |
Primary citation | McTigue, M.A.,Wickersham, J.A.,Pinko, C.,Showalter, R.E.,Parast, C.V.,Tempczyk-Russell, A.,Gehring, M.R.,Mroczkowski, B.,Kan, C.C.,Villafranca, J.E.,Appelt, K. Crystal structure of the kinase domain of human vascular endothelial growth factor receptor 2: a key enzyme in angiogenesis. Structure Fold.Des., 7:319-330, 1999 Cited by PubMed Abstract: Angiogenesis is involved in tumor growth, macular degeneration, retinopathy and other diseases. Vascular endothelial growth factor (VEGF) stimulates angiogenesis by binding to specific receptors (VEGFRs) on the surface of vascular endothelial cells. VEGFRs are receptor tyrosine kinases that, like the platelet-derived growth factor receptors (PDGFRs), contain a large insert within the kinase domain. PubMed: 10368301DOI: 10.1016/S0969-2126(99)80042-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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