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1VR2

HUMAN VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 (KDR) KINASE DOMAIN

Summary for 1VR2
Entry DOI10.2210/pdb1vr2/pdb
DescriptorPROTEIN (VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR KINASE) (2 entities in total)
Functional Keywordstyrosine kinase, transferase
Biological sourceHomo sapiens (human)
More
Cellular locationCell junction . Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted . Isoform 3: Secreted: P35968
Total number of polymer chains1
Total formula weight36274.74
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 citationMcTigue, 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: 10368301
DOI: 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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