Vascular Endothelial Growth Factor Receptor - Revision history

Michal Harel at 09:39, 19 January 2022

2022-01-19T09:39:46Z

←Older revision		Revision as of 09:39, 19 January 2022
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	[[Image: VEGF_receptors.png\|250px\|left\|thumb\| Interaction of VEGFs with VEGFRs. Colored arrows indicate major pathway. Black arrows indicate minor pathway.]]		[[Image: VEGF_receptors.png\|250px\|left\|thumb\| Interaction of VEGFs with VEGFRs. Colored arrows indicate major pathway. Black arrows indicate minor pathway.]]
	{{Clear}}		{{Clear}}
		+
		+	See also [[Kinase-linked, enzyme-linked and related receptors]].

	==Biological Function ==		==Biological Function ==

Alexander Berchansky at 13:40, 2 March 2021

2021-03-02T13:40:29Z

←Older revision		Revision as of 13:40, 2 March 2021
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	<StructureSection load='' size='350' side='right' scene='41/411436/Cv/1' caption='Human VEGFR kinase domain complex with anti-tumor inhibitor and sulfate (PDB code [[3c7q]])'>		<StructureSection load='' size='350' side='right' scene='41/411436/Cv/1' caption='Human VEGFR kinase domain complex with anti-tumor inhibitor and sulfate (PDB code [[3c7q]])'>
	==Introduction==		==Introduction==
-	[[Vascular Endothelial Growth Factor Receptor]]s (VEGFRs) are tyrosine kinase receptors responsible for binding with [[VEGF]] to initiate signal cascades that stimulate angiogenesis among other effects<ref>PMID:22130231</ref>. VEGFRs convey signals to other signal transduction effectors via autophosphorylation of specific residues in its structure. Because VEGFRs are up-regulated in cancerous tumors which have a high metabolic need for oxygen, VEGFRs are an important target for [[pharmaceutical drugs]] treating [[cancer]]. VEGFR subtypes are numbered 1,2,3.	+	[[Vascular Endothelial Growth Factor Receptor]]s (VEGFRs) are [[tyrosine kinase receptors]] responsible for binding with [[VEGF]] to initiate signal cascades that stimulate angiogenesis among other effects<ref>PMID:22130231</ref>. VEGFRs convey signals to other signal transduction effectors via autophosphorylation of specific residues in its structure. Because VEGFRs are up-regulated in cancerous tumors which have a high metabolic need for oxygen, VEGFRs are an important target for [[pharmaceutical drugs]] treating [[cancer]]. VEGFR subtypes are numbered 1,2,3.
	[[Image: VEGF_receptors.png\|250px\|left\|thumb\| Interaction of VEGFs with VEGFRs. Colored arrows indicate major pathway. Black arrows indicate minor pathway.]]		[[Image: VEGF_receptors.png\|250px\|left\|thumb\| Interaction of VEGFs with VEGFRs. Colored arrows indicate major pathway. Black arrows indicate minor pathway.]]
	{{Clear}}		{{Clear}}

Michal Harel at 07:17, 3 February 2021

2021-02-03T07:17:47Z

←Older revision		Revision as of 07:17, 3 February 2021
Line 25:		Line 25:
	*<scene name='41/411436/Cv/4'>Anti-tumor inhibitor binding site</scene> (PDB code [[3c7q]]).		*<scene name='41/411436/Cv/4'>Anti-tumor inhibitor binding site</scene> (PDB code [[3c7q]]).
	<br />		<br />
-	[[3D structures of vascular endothelial growth factor receptor]]	+	==[[3D structures of vascular endothelial growth factor receptor]]==
	</StructureSection>		</StructureSection>
	__NOTOC__		__NOTOC__

Michal Harel at 07:16, 3 February 2021

2021-02-03T07:16:49Z

←Older revision		Revision as of 07:16, 3 February 2021
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	</StructureSection>		</StructureSection>
	__NOTOC__		__NOTOC__
-	== 3D Structures of VEGFR==
-
-	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-	{{#tree:id=OrganizedByTopic\|openlevels=0\|
-
-	*VEGFR-1; Domains - 2 37-137; 1-6 27-656; kinase 801-1158
-
-	**[[1rv6]] - hVEGFR-1 domain 2 + PlGF - human <br />
-	**[[4ckv]] - hVEGFR-1 domain 2 + Zn<br />
-	**[[4cl7]] - hVEGFR-1 domain 2 + Co<br />
-	**[[5abd]] - hVEGFR-1 domain 2 + Cu<br />
-	**[[2xac]] – hVEGFR-1 domain 2 + hVEGF-B<br />
-	**[[1qsv]], [[1qsz]] - hVEGFR-1 VEGF-binding domain 129-229 – NMR<br />
-	**[[5t89]] – hVEGFR-1 domains 1-6 + hVEGF-A<br />
-	**[[3hng]] - hVEGFR-1 kinase domain + N-(4-Chlorophenyl)-2-((pyridin-4-ylmethyl)amino)benzamid <br />
-
-	*VEGFR-2; Domains - D2 112-215; D3 220-338; D4-D5 326-549; D7 657-764; transmembrane 759-795; kinase 806-1171
-
-	**[[3kvq]] - hVEGFR-2 D7 domain <br />
-	**[[1vr2]] - hVEGFR-2 kinase domain (mutant)<br />
-	**[[2m59]], [[2met]], [[2meu]] - hVEGFR-2 transmembrane domain – NMR<br />
-	**[[2x1w]], [[2x1x]] – hVEGFR-2 D2 domain + hVEGF-C<br />
-	**[[3v2a]] - hVEGFR-2 D1-D7 domain 1-764 + hVEGF-A<br />
-	**[[3v6b]] - hVEGFR-2 D2-D5 domain + hVEGF-E<br />
-	**[[3efl]], [[4ag8]], [[4agc]], [[4agd]], [[4asd]], [[4ase]], [[3vo3]], [[3wzd]], [[3wze]], [[5ew3]] - hVEGFR-2 kinase domain (mutant) + cancer drug<br />
-	**[[3ewh]], [[3cjf]], [[3cjg]], [[3vhe]] - hVEGFR-2 kinase domain + pyrimidine derivative<br />
-	**[[3c7q]] - hVEGFR-2 kinase domain + BIBF1120<br />
-	**[[3cp9]], [[3cpb]], [[3cpc]], [[3be2]], [[3b8q]], [[3b8r]], [[2qu5]], [[2qu6]], [[2p2h]], [[2p2i]], [[1ywn]], [[1y6a]], [[1y6b]],[[3vid]], [[3vhk]], [[3dtw]], [[3gqo]], [[3gqq]], [[6gqp]], [[6gqo]], [[6gqq]] - hVEGFR-2 kinase domain + inhibitor<br />
-	**[[2oh4]], [[2rl5]], [[2xir]], [[3u6j]], [[3vnt]], [[6xvj]], [[6xvk]] - hVEGFR-2 kinase domain (mutant)+ inhibitor<br />
-	**[[3s35]], [[3s36]], [[3s37]] - hVEGFR-2 D3 domain + Fab heavy+light chains<br />
-	**[[5oyj]] - hVEGFR-2 D4-D5 domain + DARPin<br />
-
-	*VEGFR-3
-
-	**[[4bsj]] - hVEGFR-3 extracellular domain 4 & 5<br />
-	**[[4bsk]] - hVEGFR-3 extracellular domain 1 & 2 + VEGF-C<br />
-
-	*VEGF 165 receptor (neuropilin) see [[Neuropilin]]
-	}}

	==Additional Resources==		==Additional Resources==

Michal Harel at 07:11, 3 February 2021

2021-02-03T07:11:53Z

←Older revision		Revision as of 07:11, 3 February 2021
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	*<scene name='41/411436/Cv/4'>Anti-tumor inhibitor binding site</scene> (PDB code [[3c7q]]).		*<scene name='41/411436/Cv/4'>Anti-tumor inhibitor binding site</scene> (PDB code [[3c7q]]).
	<br />		<br />
		+	[[3D structures of vascular endothelial growth factor receptor]]
	</StructureSection>		</StructureSection>
	__NOTOC__		__NOTOC__

Michal Harel at 07:22, 11 January 2021

2021-01-11T07:22:08Z

Michal Harel at 09:38, 25 March 2020

2020-03-25T09:38:43Z

Michal Harel at 21:21, 5 October 2018

2018-10-05T21:21:46Z

←Older revision		Revision as of 21:21, 5 October 2018
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	**[[3hng]] - hVEGFR-1 kinase domain + N-(4-Chlorophenyl)-2-((pyridin-4-ylmethyl)amino)benzamid <br />		**[[3hng]] - hVEGFR-1 kinase domain + N-(4-Chlorophenyl)-2-((pyridin-4-ylmethyl)amino)benzamid <br />

-	*VEGFR-2	+	*VEGFR-2; Domains - D2 112-215; D3 220-338; D4-D5 326-549; D7 657-764; transmembrane 759-795; kinase 806-1171

-	**[[3kvq]] - hVEGFR-2 ~~extracellular~~ domain 7<br />	+	**[[3kvq]] - hVEGFR-2 D7 domain <br />
	**[[1vr2]] - hVEGFR-2 kinase domain (mutant)<br />		**[[1vr2]] - hVEGFR-2 kinase domain (mutant)<br />
	**[[2m59]], [[2met]], [[2meu]] - hVEGFR-2 transmembrane domain – NMR<br />		**[[2m59]], [[2met]], [[2meu]] - hVEGFR-2 transmembrane domain – NMR<br />
-	**[[2x1w]], [[2x1x]] – hVEGFR-2 ~~IG-like domains 2 & 3~~ +hVEGF-C<br />	+	**[[2x1w]], [[2x1x]] – hVEGFR-2 D2 domain + hVEGF-C<br />
-	**[[3v2a]] - hVEGFR-2 + hVEGF-A<br />	+	**[[3v2a]] - hVEGFR-2 D1-D7 domain + hVEGF-A<br />
-	**[[3v6b]] - hVEGFR-2 ~~residues 132~~-~~548~~ + hVEGF-E<br />	+	**[[3v6b]] - hVEGFR-2 D2-D5 domain + hVEGF-E<br />
	**[[3efl]] – hVEGFR-2 kinase domain (mutant)+ motesanib <br />		**[[3efl]] – hVEGFR-2 kinase domain (mutant)+ motesanib <br />
	**[[4ag8]], [[4agc]], [[4agd]], [[4asd]], [[4ase]], [[3vo3]], [[3wzd]], [[3wze]], [[5ew3]] - hVEGFR-2 kinase domain (mutant) + cancer drug<br />		**[[4ag8]], [[4agc]], [[4agd]], [[4asd]], [[4ase]], [[3vo3]], [[3wzd]], [[3wze]], [[5ew3]] - hVEGFR-2 kinase domain (mutant) + cancer drug<br />
	**[[3ewh]], [[3cjf]], [[3cjg]], [[3vhe]] - hVEGFR-2 kinase domain + pyrimidine derivative<br />		**[[3ewh]], [[3cjf]], [[3cjg]], [[3vhe]] - hVEGFR-2 kinase domain + pyrimidine derivative<br />
	**[[3c7q]] - hVEGFR-2 kinase domain + BIBF1120<br />		**[[3c7q]] - hVEGFR-2 kinase domain + BIBF1120<br />
-	**[[3dtw]] - hVEGFR-2 kinase domain + benzisoxazole <br />	+	**[[3cp9]], [[3cpb]], [[3cpc]], [[3be2]], [[3b8q]], [[3b8r]], [[2qu5]], [[2qu6]], [[2p2h]], [[2p2i]], [[1ywn]], [[1y6a]], [[1y6b]],[[3vid]], [[3vhk]], [[3dtw]], [[3gqo]], [[3gqq]], [[6gqp]] - hVEGFR-2 kinase domain + inhibitor<br />
-	**[[3cp9]], [[3cpb]], [[3cpc]], [[3be2]], [[3b8q]], [[3b8r]], [[2qu5]], [[2qu6]], [[2p2h]], [[2p2i]], [[1ywn]], [[1y6a]], [[1y6b]],[[3vid]], [[3vhk]] - hVEGFR-2 kinase domain + inhibitor<br />	+
	**[[2oh4]], [[2rl5]], [[2xir]], [[3u6j]], [[3vnt]] - hVEGFR-2 kinase domain (mutant)+ inhibitor<br />		**[[2oh4]], [[2rl5]], [[2xir]], [[3u6j]], [[3vnt]] - hVEGFR-2 kinase domain (mutant)+ inhibitor<br />
-	**[[3s35]], [[3s36]], [[3s37]] - hVEGFR-2 ~~extracellular~~ domain 3 + Fab heavy+light chains	+	**[[3s35]], [[3s36]], [[3s37]] - hVEGFR-2 D3 domain + Fab heavy+light chains<br />
		+	**[[5oyj]] - hVEGFR-2 D4-D5 domain + DARPin<br />

	*VEGFR-3		*VEGFR-3

Michal Harel at 20:49, 5 October 2018

2018-10-05T20:49:21Z

←Older revision		Revision as of 20:49, 5 October 2018
Line 1:		Line 1:
-	<StructureSection load='' size='~~450~~' side='right' scene='41/411436/Cv/1' caption='Human VEGFR kinase domain complex with anti-tumor inhibitor and sulfate (PDB code [[3c7q]])'>	+	<StructureSection load='' size='350' side='right' scene='41/411436/Cv/1' caption='Human VEGFR kinase domain complex with anti-tumor inhibitor and sulfate (PDB code [[3c7q]])'>
	==Introduction==		==Introduction==
-	[[Vascular Endothelial Growth Factor Receptor]]s (VEGFRs) are tyrosine kinase receptors responsible for binding with [[VEGF]] to initiate signal cascades that stimulate angiogenesis among other effects. VEGFRs convey signals to other signal transduction effectors via autophosphorylation of specific residues in its structure. Because VEGFRs are up-regulated in cancerous tumors which have a high metabolic need for oxygen, VEGFRs are an important target for [[pharmaceutical drugs]] treating [[cancer]]. VEGFR subtypes are numbered 1,2,3.	+	[[Vascular Endothelial Growth Factor Receptor]]s (VEGFRs) are tyrosine kinase receptors responsible for binding with [[VEGF]] to initiate signal cascades that stimulate angiogenesis among other effects<ref>PMID:22130231</ref>. VEGFRs convey signals to other signal transduction effectors via autophosphorylation of specific residues in its structure. Because VEGFRs are up-regulated in cancerous tumors which have a high metabolic need for oxygen, VEGFRs are an important target for [[pharmaceutical drugs]] treating [[cancer]]. VEGFR subtypes are numbered 1,2,3.
	[[Image: VEGF_receptors.png\|250px\|left\|thumb\| Interaction of VEGFs with VEGFRs. Colored arrows indicate major pathway. Black arrows indicate minor pathway.]]		[[Image: VEGF_receptors.png\|250px\|left\|thumb\| Interaction of VEGFs with VEGFRs. Colored arrows indicate major pathway. Black arrows indicate minor pathway.]]
	{{Clear}}		{{Clear}}

Joel L. Sussman at 20:18, 9 November 2017

2017-11-09T20:18:43Z

←Older revision		Revision as of 20:18, 9 November 2017
Line 1:		Line 1:
-	<StructureSection load='~~3c7q~~' size='450' side='right' scene='41/411436/Cv/1' caption='Human VEGFR kinase domain complex with anti-tumor inhibitor and sulfate (PDB code [[3c7q]])'>	+	<StructureSection load='' size='450' side='right' scene='41/411436/Cv/1' caption='Human VEGFR kinase domain complex with anti-tumor inhibitor and sulfate (PDB code [[3c7q]])'>
	==Introduction==		==Introduction==
	[[Vascular Endothelial Growth Factor Receptor]]s (VEGFRs) are tyrosine kinase receptors responsible for binding with [[VEGF]] to initiate signal cascades that stimulate angiogenesis among other effects. VEGFRs convey signals to other signal transduction effectors via autophosphorylation of specific residues in its structure. Because VEGFRs are up-regulated in cancerous tumors which have a high metabolic need for oxygen, VEGFRs are an important target for [[pharmaceutical drugs]] treating [[cancer]]. VEGFR subtypes are numbered 1,2,3.		[[Vascular Endothelial Growth Factor Receptor]]s (VEGFRs) are tyrosine kinase receptors responsible for binding with [[VEGF]] to initiate signal cascades that stimulate angiogenesis among other effects. VEGFRs convey signals to other signal transduction effectors via autophosphorylation of specific residues in its structure. Because VEGFRs are up-regulated in cancerous tumors which have a high metabolic need for oxygen, VEGFRs are an important target for [[pharmaceutical drugs]] treating [[cancer]]. VEGFR subtypes are numbered 1,2,3.

←Older revision		Revision as of 07:22, 11 January 2021
Line 39:		Line 39:
	**[[5abd]] - hVEGFR-1 domain 2 + Cu<br />		**[[5abd]] - hVEGFR-1 domain 2 + Cu<br />
	**[[2xac]] – hVEGFR-1 domain 2 + hVEGF-B<br />		**[[2xac]] – hVEGFR-1 domain 2 + hVEGF-B<br />
-	**[[1qsv]] - hVEGFR-1 VEGF-binding domain 129-229 – NMR<br />	+	**[[1qsv]], [[1qsz]] - hVEGFR-1 VEGF-binding domain 129-229 – NMR<br />
	**[[5t89]] – hVEGFR-1 domains 1-6 + hVEGF-A<br />		**[[5t89]] – hVEGFR-1 domains 1-6 + hVEGF-A<br />
	**[[3hng]] - hVEGFR-1 kinase domain + N-(4-Chlorophenyl)-2-((pyridin-4-ylmethyl)amino)benzamid <br />		**[[3hng]] - hVEGFR-1 kinase domain + N-(4-Chlorophenyl)-2-((pyridin-4-ylmethyl)amino)benzamid <br />
Line 51:		Line 51:
	**[[3v2a]] - hVEGFR-2 D1-D7 domain 1-764 + hVEGF-A<br />		**[[3v2a]] - hVEGFR-2 D1-D7 domain 1-764 + hVEGF-A<br />
	**[[3v6b]] - hVEGFR-2 D2-D5 domain + hVEGF-E<br />		**[[3v6b]] - hVEGFR-2 D2-D5 domain + hVEGF-E<br />
-	**[[3efl]] ~~– hVEGFR-2 kinase domain (mutant)+ motesanib <br />~~	+	**[[3efl]], [[4ag8]], [[4agc]], [[4agd]], [[4asd]], [[4ase]], [[3vo3]], [[3wzd]], [[3wze]], [[5ew3]] - hVEGFR-2 kinase domain (mutant) + cancer drug<br />
-	**[[4ag8]], [[4agc]], [[4agd]], [[4asd]], [[4ase]], [[3vo3]], [[3wzd]], [[3wze]], [[5ew3]] - hVEGFR-2 kinase domain (mutant) + cancer drug<br />	+
	**[[3ewh]], [[3cjf]], [[3cjg]], [[3vhe]] - hVEGFR-2 kinase domain + pyrimidine derivative<br />		**[[3ewh]], [[3cjf]], [[3cjg]], [[3vhe]] - hVEGFR-2 kinase domain + pyrimidine derivative<br />
	**[[3c7q]] - hVEGFR-2 kinase domain + BIBF1120<br />		**[[3c7q]] - hVEGFR-2 kinase domain + BIBF1120<br />
	**[[3cp9]], [[3cpb]], [[3cpc]], [[3be2]], [[3b8q]], [[3b8r]], [[2qu5]], [[2qu6]], [[2p2h]], [[2p2i]], [[1ywn]], [[1y6a]], [[1y6b]],[[3vid]], [[3vhk]], [[3dtw]], [[3gqo]], [[3gqq]], [[6gqp]], [[6gqo]], [[6gqq]] - hVEGFR-2 kinase domain + inhibitor<br />		**[[3cp9]], [[3cpb]], [[3cpc]], [[3be2]], [[3b8q]], [[3b8r]], [[2qu5]], [[2qu6]], [[2p2h]], [[2p2i]], [[1ywn]], [[1y6a]], [[1y6b]],[[3vid]], [[3vhk]], [[3dtw]], [[3gqo]], [[3gqq]], [[6gqp]], [[6gqo]], [[6gqq]] - hVEGFR-2 kinase domain + inhibitor<br />
-	**[[2oh4]], [[2rl5]], [[2xir]], [[3u6j]], [[3vnt]] - hVEGFR-2 kinase domain (mutant)+ inhibitor<br />	+	**[[2oh4]], [[2rl5]], [[2xir]], [[3u6j]], [[3vnt]], [[6xvj]], [[6xvk]] - hVEGFR-2 kinase domain (mutant)+ inhibitor<br />
	**[[3s35]], [[3s36]], [[3s37]] - hVEGFR-2 D3 domain + Fab heavy+light chains<br />		**[[3s35]], [[3s36]], [[3s37]] - hVEGFR-2 D3 domain + Fab heavy+light chains<br />
	**[[5oyj]] - hVEGFR-2 D4-D5 domain + DARPin<br />		**[[5oyj]] - hVEGFR-2 D4-D5 domain + DARPin<br />

←Older revision		Revision as of 09:38, 25 March 2020
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	{{#tree:id=OrganizedByTopic\|openlevels=0\|		{{#tree:id=OrganizedByTopic\|openlevels=0\|

-	*VEGFR-1	+	*VEGFR-1; Domains - 2 37-137; 1-6 27-656; kinase 801-1158

	**[[1rv6]] - hVEGFR-1 domain 2 + PlGF - human <br />		**[[1rv6]] - hVEGFR-1 domain 2 + PlGF - human <br />
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	**[[4cl7]] - hVEGFR-1 domain 2 + Co<br />		**[[4cl7]] - hVEGFR-1 domain 2 + Co<br />
	**[[5abd]] - hVEGFR-1 domain 2 + Cu<br />		**[[5abd]] - hVEGFR-1 domain 2 + Cu<br />
-	**[[1qsv]] - hVEGFR-1 VEGF-binding domain – NMR<br />
	**[[2xac]] – hVEGFR-1 domain 2 + hVEGF-B<br />		**[[2xac]] – hVEGFR-1 domain 2 + hVEGF-B<br />
		+	**[[1qsv]] - hVEGFR-1 VEGF-binding domain 129-229 – NMR<br />
	**[[5t89]] – hVEGFR-1 domains 1-6 + hVEGF-A<br />		**[[5t89]] – hVEGFR-1 domains 1-6 + hVEGF-A<br />
	**[[3hng]] - hVEGFR-1 kinase domain + N-(4-Chlorophenyl)-2-((pyridin-4-ylmethyl)amino)benzamid <br />		**[[3hng]] - hVEGFR-1 kinase domain + N-(4-Chlorophenyl)-2-((pyridin-4-ylmethyl)amino)benzamid <br />
Line 49:		Line 49:
	**[[2m59]], [[2met]], [[2meu]] - hVEGFR-2 transmembrane domain – NMR<br />		**[[2m59]], [[2met]], [[2meu]] - hVEGFR-2 transmembrane domain – NMR<br />
	**[[2x1w]], [[2x1x]] – hVEGFR-2 D2 domain + hVEGF-C<br />		**[[2x1w]], [[2x1x]] – hVEGFR-2 D2 domain + hVEGF-C<br />
-	**[[3v2a]] - hVEGFR-2 D1-D7 domain + hVEGF-A<br />	+	**[[3v2a]] - hVEGFR-2 D1-D7 domain 1-764 + hVEGF-A<br />
	**[[3v6b]] - hVEGFR-2 D2-D5 domain + hVEGF-E<br />		**[[3v6b]] - hVEGFR-2 D2-D5 domain + hVEGF-E<br />
	**[[3efl]] – hVEGFR-2 kinase domain (mutant)+ motesanib <br />		**[[3efl]] – hVEGFR-2 kinase domain (mutant)+ motesanib <br />
Line 55:		Line 55:
	**[[3ewh]], [[3cjf]], [[3cjg]], [[3vhe]] - hVEGFR-2 kinase domain + pyrimidine derivative<br />		**[[3ewh]], [[3cjf]], [[3cjg]], [[3vhe]] - hVEGFR-2 kinase domain + pyrimidine derivative<br />
	**[[3c7q]] - hVEGFR-2 kinase domain + BIBF1120<br />		**[[3c7q]] - hVEGFR-2 kinase domain + BIBF1120<br />
-	**[[3cp9]], [[3cpb]], [[3cpc]], [[3be2]], [[3b8q]], [[3b8r]], [[2qu5]], [[2qu6]], [[2p2h]], [[2p2i]], [[1ywn]], [[1y6a]], [[1y6b]],[[3vid]], [[3vhk]], [[3dtw]], [[3gqo]], [[3gqq]], [[6gqp]] - hVEGFR-2 kinase domain + inhibitor<br />	+	**[[3cp9]], [[3cpb]], [[3cpc]], [[3be2]], [[3b8q]], [[3b8r]], [[2qu5]], [[2qu6]], [[2p2h]], [[2p2i]], [[1ywn]], [[1y6a]], [[1y6b]],[[3vid]], [[3vhk]], [[3dtw]], [[3gqo]], [[3gqq]], [[6gqp]], [[6gqo]], [[6gqq]] - hVEGFR-2 kinase domain + inhibitor<br />
	**[[2oh4]], [[2rl5]], [[2xir]], [[3u6j]], [[3vnt]] - hVEGFR-2 kinase domain (mutant)+ inhibitor<br />		**[[2oh4]], [[2rl5]], [[2xir]], [[3u6j]], [[3vnt]] - hVEGFR-2 kinase domain (mutant)+ inhibitor<br />
	**[[3s35]], [[3s36]], [[3s37]] - hVEGFR-2 D3 domain + Fab heavy+light chains<br />		**[[3s35]], [[3s36]], [[3s37]] - hVEGFR-2 D3 domain + Fab heavy+light chains<br />