2py3 - Revision history

OCA at 11:11, 30 August 2023

2023-08-30T11:11:54Z

← Older revision		Revision as of 11:11, 30 August 2023
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	<StructureSection load='2py3' size='340' side='right'caption='[[2py3]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2py3' size='340' side='right'caption='[[2py3]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.3Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[2psq\|2psq]], [[2pvf\|2pvf]], [[2pvy\|2pvy]], [[2pwl\|2pwl]], [[2pz5\|2pz5]], [[2pzp\|2pzp]], [[2pzr\|2pzr]], [[2q0b\|2q0b]]~~</~~div~~><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></~~td><td class="sblockDat"~~>~~FGFR2~~, ~~BEK, KSAM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~<~~/td></tr>~~
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1]~~ </~~span~~></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [https://pdbe.org/2py3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [https://www.ebi.ac.uk/pdbsum/2py3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2py3 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [https://pdbe.org/2py3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [https://www.ebi.ac.uk/pdbsum/2py3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2py3 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN]] Defects in FGFR2 are the cause of Crouzon syndrome (CS) [MIM:[https://omim.org/entry/123500 123500]]; also called craniofacial dysostosis type I (CFD1). CS is an autosomal dominant syndrome characterized by craniosynostosis (premature fusion of the skull sutures), hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> [:]<ref>PMID:7581378</ref> <ref>PMID:7987400</ref> <ref>PMID:7874170</ref> <ref>PMID:7655462</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:8946174</ref> <ref>PMID:8956050</ref> <ref>PMID:9002682</ref> <ref>PMID:9152842</ref> <ref>PMID:9677057</ref> <ref>PMID:9521581</ref> <ref>PMID:10574673</ref> <ref>PMID:11173845</ref> <ref>PMID:11380921</ref> <ref>PMID:11781872</ref> Defects in FGFR2 are a cause of Jackson-Weiss syndrome (JWS) [MIM:[https://omim.org/entry/123150 123150]]. JWS is an autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence.<ref>PMID:19387476</ref> <ref>PMID:7874170</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:9677057</ref> <ref>PMID:9385368</ref> Defects in FGFR2 are a cause of Apert syndrome (APRS) [MIM:[https://omim.org/entry/101200 101200]]; also known as acrocephalosyndactyly type 1 (ACS1). APRS is a syndrome characterized by facio-cranio-synostosis, osseous and membranous syndactyly of the four extremities, and midface hypoplasia. The craniosynostosis is bicoronal and results in acrocephaly of brachysphenocephalic type. Syndactyly of the fingers and toes may be total (mitten hands and sock feet) or partial affecting the second, third, and fourth digits. Intellectual deficit is frequent and often severe, usually being associated with cerebral malformations.<ref>PMID:15190072</ref> <ref>PMID:19387476</ref> <ref>PMID:9002682</ref> <ref>PMID:9677057</ref> <ref>PMID:11781872</ref> <ref>PMID:7668257</ref> <ref>PMID:11390973</ref> <ref>PMID:7719344</ref> <ref>PMID:9452027</ref> Defects in FGFR2 are a cause of Pfeiffer syndrome (PS) [MIM:[https://omim.org/entry/101600 101600]]; also known as acrocephalosyndactyly type V (ACS5). PS is characterized by craniosynostosis (premature fusion of the skull sutures) with deviation and enlargement of the thumbs and great toes, brachymesophalangy, with phalangeal ankylosis and a varying degree of soft tissue syndactyly. Three subtypes of Pfeiffer syndrome have been described: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3).<ref>PMID:16844695</ref> <ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:8644708</ref> <ref>PMID:9002682</ref> <ref>PMID:11173845</ref> <ref>PMID:11781872</ref> <ref>PMID:7719333</ref> <ref>PMID:7719345</ref> <ref>PMID:9150725</ref> <ref>PMID:9693549</ref> <ref>PMID:9719378</ref> <ref>PMID:10394936</ref> <ref>PMID:10945669</ref> Defects in FGFR2 are the cause of Beare-Stevenson cutis gyrata syndrome (BSCGS) [MIM:[https://omim.org/entry/123790 123790]]. BSCGS is an autosomal dominant condition is characterized by the furrowed skin disorder of cutis gyrata, acanthosis nigricans, craniosynostosis, craniofacial dysmorphism, digital anomalies, umbilical and anogenital abnormalities and early death.<ref>PMID:19387476</ref> <ref>PMID:8696350</ref> <ref>PMID:12000365</ref> Defects in FGFR2 are the cause of familial scaphocephaly syndrome (FSPC) [MIM:[https://omim.org/entry/609579 609579]]; also known as scaphocephaly with maxillary retrusion and mental retardation. FSPC is an autosomal dominant craniosynostosis syndrome characterized by scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion, and mild intellectual disability. Scaphocephaly is the most common of the craniosynostosis conditions and is characterized by a long, narrow head. It is due to premature fusion of the sagittal suture or from external deformation.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:16061565</ref> Defects in FGFR2 are a cause of lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:[https://omim.org/entry/149730 149730]]; also known as Levy-Hollister syndrome. LADDS is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. LADDS is an autosomal dominant syndrome characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed.<ref>PMID:19387476</ref> <ref>PMID:18056630</ref> <ref>PMID:16501574</ref> Defects in FGFR2 are the cause of Antley-Bixler syndrome without genital anomalies or disordered steroidogenesis (ABS2) [MIM:[https://omim.org/entry/207410 207410]]. A rare syndrome characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. Arachnodactyly and/or camptodactyly have also been reported.<ref>PMID:19387476</ref> <ref>PMID:10633130</ref> Defects in FGFR2 are the cause of Bent bone dysplasia syndrome (BBDS) [MIM:[https://omim.org/entry/614592 614592]]. BBDS is a perinatal lethal skeletal dysplasia characterized by poor mineralization of the calvarium, craniosynostosis, dysmorphic facial features, prenatal teeth, hypoplastic pubis and clavicles, osteopenia, and bent long bones. Dysmorphic facial features included low-set ears, hypertelorism, midface hypoplasia, prematurely erupted fetal teeth, and micrognathia.<ref>PMID:19387476</ref> <ref>PMID:22387015</ref>		[https://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN] Defects in FGFR2 are the cause of Crouzon syndrome (CS) [MIM:[https://omim.org/entry/123500 123500]; also called craniofacial dysostosis type I (CFD1). CS is an autosomal dominant syndrome characterized by craniosynostosis (premature fusion of the skull sutures), hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> [:]<ref>PMID:7581378</ref> <ref>PMID:7987400</ref> <ref>PMID:7874170</ref> <ref>PMID:7655462</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:8946174</ref> <ref>PMID:8956050</ref> <ref>PMID:9002682</ref> <ref>PMID:9152842</ref> <ref>PMID:9677057</ref> <ref>PMID:9521581</ref> <ref>PMID:10574673</ref> <ref>PMID:11173845</ref> <ref>PMID:11380921</ref> <ref>PMID:11781872</ref> Defects in FGFR2 are a cause of Jackson-Weiss syndrome (JWS) [MIM:[https://omim.org/entry/123150 123150]. JWS is an autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence.<ref>PMID:19387476</ref> <ref>PMID:7874170</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:9677057</ref> <ref>PMID:9385368</ref> Defects in FGFR2 are a cause of Apert syndrome (APRS) [MIM:[https://omim.org/entry/101200 101200]; also known as acrocephalosyndactyly type 1 (ACS1). APRS is a syndrome characterized by facio-cranio-synostosis, osseous and membranous syndactyly of the four extremities, and midface hypoplasia. The craniosynostosis is bicoronal and results in acrocephaly of brachysphenocephalic type. Syndactyly of the fingers and toes may be total (mitten hands and sock feet) or partial affecting the second, third, and fourth digits. Intellectual deficit is frequent and often severe, usually being associated with cerebral malformations.<ref>PMID:15190072</ref> <ref>PMID:19387476</ref> <ref>PMID:9002682</ref> <ref>PMID:9677057</ref> <ref>PMID:11781872</ref> <ref>PMID:7668257</ref> <ref>PMID:11390973</ref> <ref>PMID:7719344</ref> <ref>PMID:9452027</ref> Defects in FGFR2 are a cause of Pfeiffer syndrome (PS) [MIM:[https://omim.org/entry/101600 101600]; also known as acrocephalosyndactyly type V (ACS5). PS is characterized by craniosynostosis (premature fusion of the skull sutures) with deviation and enlargement of the thumbs and great toes, brachymesophalangy, with phalangeal ankylosis and a varying degree of soft tissue syndactyly. Three subtypes of Pfeiffer syndrome have been described: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3).<ref>PMID:16844695</ref> <ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:8644708</ref> <ref>PMID:9002682</ref> <ref>PMID:11173845</ref> <ref>PMID:11781872</ref> <ref>PMID:7719333</ref> <ref>PMID:7719345</ref> <ref>PMID:9150725</ref> <ref>PMID:9693549</ref> <ref>PMID:9719378</ref> <ref>PMID:10394936</ref> <ref>PMID:10945669</ref> Defects in FGFR2 are the cause of Beare-Stevenson cutis gyrata syndrome (BSCGS) [MIM:[https://omim.org/entry/123790 123790]. BSCGS is an autosomal dominant condition is characterized by the furrowed skin disorder of cutis gyrata, acanthosis nigricans, craniosynostosis, craniofacial dysmorphism, digital anomalies, umbilical and anogenital abnormalities and early death.<ref>PMID:19387476</ref> <ref>PMID:8696350</ref> <ref>PMID:12000365</ref> Defects in FGFR2 are the cause of familial scaphocephaly syndrome (FSPC) [MIM:[https://omim.org/entry/609579 609579]; also known as scaphocephaly with maxillary retrusion and mental retardation. FSPC is an autosomal dominant craniosynostosis syndrome characterized by scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion, and mild intellectual disability. Scaphocephaly is the most common of the craniosynostosis conditions and is characterized by a long, narrow head. It is due to premature fusion of the sagittal suture or from external deformation.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:16061565</ref> Defects in FGFR2 are a cause of lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:[https://omim.org/entry/149730 149730]; also known as Levy-Hollister syndrome. LADDS is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. LADDS is an autosomal dominant syndrome characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed.<ref>PMID:19387476</ref> <ref>PMID:18056630</ref> <ref>PMID:16501574</ref> Defects in FGFR2 are the cause of Antley-Bixler syndrome without genital anomalies or disordered steroidogenesis (ABS2) [MIM:[https://omim.org/entry/207410 207410]. A rare syndrome characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. Arachnodactyly and/or camptodactyly have also been reported.<ref>PMID:19387476</ref> <ref>PMID:10633130</ref> Defects in FGFR2 are the cause of Bent bone dysplasia syndrome (BBDS) [MIM:[https://omim.org/entry/614592 614592]. BBDS is a perinatal lethal skeletal dysplasia characterized by poor mineralization of the calvarium, craniosynostosis, dysmorphic facial features, prenatal teeth, hypoplastic pubis and clavicles, osteopenia, and bent long bones. Dysmorphic facial features included low-set ears, hypertelorism, midface hypoplasia, prematurely erupted fetal teeth, and micrognathia.<ref>PMID:19387476</ref> <ref>PMID:22387015</ref>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN]] Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1.<ref>PMID:8961926</ref> <ref>PMID:8663044</ref> <ref>PMID:12529371</ref> <ref>PMID:15190072</ref> <ref>PMID:15629145</ref> <ref>PMID:16597617</ref> <ref>PMID:16844695</ref> <ref>PMID:17623664</ref> <ref>PMID:17311277</ref> <ref>PMID:18374639</ref> <ref>PMID:19410646</ref> <ref>PMID:19103595</ref> <ref>PMID:21596750</ref> <ref>PMID:19387476</ref> <ref>PMID:16384934</ref>		[https://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN] Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1.<ref>PMID:8961926</ref> <ref>PMID:8663044</ref> <ref>PMID:12529371</ref> <ref>PMID:15190072</ref> <ref>PMID:15629145</ref> <ref>PMID:16597617</ref> <ref>PMID:16844695</ref> <ref>PMID:17623664</ref> <ref>PMID:17311277</ref> <ref>PMID:18374639</ref> <ref>PMID:19410646</ref> <ref>PMID:19103595</ref> <ref>PMID:21596750</ref> <ref>PMID:19387476</ref> <ref>PMID:16384934</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: Receptor protein-tyrosine kinase]]~~		[[Category: Chen H]]
	[[Category: Chen, H]]		[[Category: Mohammadi M]]
	[[Category: Mohammadi, M]]
	~~[[Category: Kinase domain fold consisting of n- and c-lobe]]~~
	~~[[Category: Transferase~~]]

OCA at 15:36, 17 June 2021

2021-06-17T15:36:00Z

← Older revision		Revision as of 15:36, 17 June 2021
Line 1:		Line 1:

	==Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome==		==Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome==
	<StructureSection load='2py3' size='340' side='right' caption='[[2py3]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2py3' size='340' side='right'caption='[[2py3]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2psq\|2psq]], [[2pvf\|2pvf]], [[2pvy\|2pvy]], [[2pwl\|2pwl]], [[2pz5\|2pz5]], [[2pzp\|2pzp]], [[2pzr\|2pzr]], [[2q0b\|2q0b]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2psq\|2psq]], [[2pvf\|2pvf]], [[2pvy\|2pvy]], [[2pwl\|2pwl]], [[2pz5\|2pz5]], [[2pzp\|2pzp]], [[2pzr\|2pzr]], [[2q0b\|2q0b]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FGFR2, BEK, KSAM ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FGFR2, BEK, KSAM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [~~http~~://pdbe.org/2py3 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2py3 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2py3 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [https://pdbe.org/2py3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [https://www.ebi.ac.uk/pdbsum/2py3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2py3 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN]] Defects in FGFR2 are the cause of Crouzon syndrome (CS) [MIM:[~~http~~://omim.org/entry/123500 123500]]; also called craniofacial dysostosis type I (CFD1). CS is an autosomal dominant syndrome characterized by craniosynostosis (premature fusion of the skull sutures), hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> [:]<ref>PMID:7581378</ref> <ref>PMID:7987400</ref> <ref>PMID:7874170</ref> <ref>PMID:7655462</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:8946174</ref> <ref>PMID:8956050</ref> <ref>PMID:9002682</ref> <ref>PMID:9152842</ref> <ref>PMID:9677057</ref> <ref>PMID:9521581</ref> <ref>PMID:10574673</ref> <ref>PMID:11173845</ref> <ref>PMID:11380921</ref> <ref>PMID:11781872</ref> Defects in FGFR2 are a cause of Jackson-Weiss syndrome (JWS) [MIM:[~~http~~://omim.org/entry/123150 123150]]. JWS is an autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence.<ref>PMID:19387476</ref> <ref>PMID:7874170</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:9677057</ref> <ref>PMID:9385368</ref> Defects in FGFR2 are a cause of Apert syndrome (APRS) [MIM:[~~http~~://omim.org/entry/101200 101200]]; also known as acrocephalosyndactyly type 1 (ACS1). APRS is a syndrome characterized by facio-cranio-synostosis, osseous and membranous syndactyly of the four extremities, and midface hypoplasia. The craniosynostosis is bicoronal and results in acrocephaly of brachysphenocephalic type. Syndactyly of the fingers and toes may be total (mitten hands and sock feet) or partial affecting the second, third, and fourth digits. Intellectual deficit is frequent and often severe, usually being associated with cerebral malformations.<ref>PMID:15190072</ref> <ref>PMID:19387476</ref> <ref>PMID:9002682</ref> <ref>PMID:9677057</ref> <ref>PMID:11781872</ref> <ref>PMID:7668257</ref> <ref>PMID:11390973</ref> <ref>PMID:7719344</ref> <ref>PMID:9452027</ref> Defects in FGFR2 are a cause of Pfeiffer syndrome (PS) [MIM:[~~http~~://omim.org/entry/101600 101600]]; also known as acrocephalosyndactyly type V (ACS5). PS is characterized by craniosynostosis (premature fusion of the skull sutures) with deviation and enlargement of the thumbs and great toes, brachymesophalangy, with phalangeal ankylosis and a varying degree of soft tissue syndactyly. Three subtypes of Pfeiffer syndrome have been described: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3).<ref>PMID:16844695</ref> <ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:8644708</ref> <ref>PMID:9002682</ref> <ref>PMID:11173845</ref> <ref>PMID:11781872</ref> <ref>PMID:7719333</ref> <ref>PMID:7719345</ref> <ref>PMID:9150725</ref> <ref>PMID:9693549</ref> <ref>PMID:9719378</ref> <ref>PMID:10394936</ref> <ref>PMID:10945669</ref> Defects in FGFR2 are the cause of Beare-Stevenson cutis gyrata syndrome (BSCGS) [MIM:[~~http~~://omim.org/entry/123790 123790]]. BSCGS is an autosomal dominant condition is characterized by the furrowed skin disorder of cutis gyrata, acanthosis nigricans, craniosynostosis, craniofacial dysmorphism, digital anomalies, umbilical and anogenital abnormalities and early death.<ref>PMID:19387476</ref> <ref>PMID:8696350</ref> <ref>PMID:12000365</ref> Defects in FGFR2 are the cause of familial scaphocephaly syndrome (FSPC) [MIM:[~~http~~://omim.org/entry/609579 609579]]; also known as scaphocephaly with maxillary retrusion and mental retardation. FSPC is an autosomal dominant craniosynostosis syndrome characterized by scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion, and mild intellectual disability. Scaphocephaly is the most common of the craniosynostosis conditions and is characterized by a long, narrow head. It is due to premature fusion of the sagittal suture or from external deformation.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:16061565</ref> Defects in FGFR2 are a cause of lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:[~~http~~://omim.org/entry/149730 149730]]; also known as Levy-Hollister syndrome. LADDS is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. LADDS is an autosomal dominant syndrome characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed.<ref>PMID:19387476</ref> <ref>PMID:18056630</ref> <ref>PMID:16501574</ref> Defects in FGFR2 are the cause of Antley-Bixler syndrome without genital anomalies or disordered steroidogenesis (ABS2) [MIM:[~~http~~://omim.org/entry/207410 207410]]. A rare syndrome characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. Arachnodactyly and/or camptodactyly have also been reported.<ref>PMID:19387476</ref> <ref>PMID:10633130</ref> Defects in FGFR2 are the cause of Bent bone dysplasia syndrome (BBDS) [MIM:[~~http~~://omim.org/entry/614592 614592]]. BBDS is a perinatal lethal skeletal dysplasia characterized by poor mineralization of the calvarium, craniosynostosis, dysmorphic facial features, prenatal teeth, hypoplastic pubis and clavicles, osteopenia, and bent long bones. Dysmorphic facial features included low-set ears, hypertelorism, midface hypoplasia, prematurely erupted fetal teeth, and micrognathia.<ref>PMID:19387476</ref> <ref>PMID:22387015</ref>		[[https://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN]] Defects in FGFR2 are the cause of Crouzon syndrome (CS) [MIM:[https://omim.org/entry/123500 123500]]; also called craniofacial dysostosis type I (CFD1). CS is an autosomal dominant syndrome characterized by craniosynostosis (premature fusion of the skull sutures), hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> [:]<ref>PMID:7581378</ref> <ref>PMID:7987400</ref> <ref>PMID:7874170</ref> <ref>PMID:7655462</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:8946174</ref> <ref>PMID:8956050</ref> <ref>PMID:9002682</ref> <ref>PMID:9152842</ref> <ref>PMID:9677057</ref> <ref>PMID:9521581</ref> <ref>PMID:10574673</ref> <ref>PMID:11173845</ref> <ref>PMID:11380921</ref> <ref>PMID:11781872</ref> Defects in FGFR2 are a cause of Jackson-Weiss syndrome (JWS) [MIM:[https://omim.org/entry/123150 123150]]. JWS is an autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence.<ref>PMID:19387476</ref> <ref>PMID:7874170</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:9677057</ref> <ref>PMID:9385368</ref> Defects in FGFR2 are a cause of Apert syndrome (APRS) [MIM:[https://omim.org/entry/101200 101200]]; also known as acrocephalosyndactyly type 1 (ACS1). APRS is a syndrome characterized by facio-cranio-synostosis, osseous and membranous syndactyly of the four extremities, and midface hypoplasia. The craniosynostosis is bicoronal and results in acrocephaly of brachysphenocephalic type. Syndactyly of the fingers and toes may be total (mitten hands and sock feet) or partial affecting the second, third, and fourth digits. Intellectual deficit is frequent and often severe, usually being associated with cerebral malformations.<ref>PMID:15190072</ref> <ref>PMID:19387476</ref> <ref>PMID:9002682</ref> <ref>PMID:9677057</ref> <ref>PMID:11781872</ref> <ref>PMID:7668257</ref> <ref>PMID:11390973</ref> <ref>PMID:7719344</ref> <ref>PMID:9452027</ref> Defects in FGFR2 are a cause of Pfeiffer syndrome (PS) [MIM:[https://omim.org/entry/101600 101600]]; also known as acrocephalosyndactyly type V (ACS5). PS is characterized by craniosynostosis (premature fusion of the skull sutures) with deviation and enlargement of the thumbs and great toes, brachymesophalangy, with phalangeal ankylosis and a varying degree of soft tissue syndactyly. Three subtypes of Pfeiffer syndrome have been described: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3).<ref>PMID:16844695</ref> <ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:8644708</ref> <ref>PMID:9002682</ref> <ref>PMID:11173845</ref> <ref>PMID:11781872</ref> <ref>PMID:7719333</ref> <ref>PMID:7719345</ref> <ref>PMID:9150725</ref> <ref>PMID:9693549</ref> <ref>PMID:9719378</ref> <ref>PMID:10394936</ref> <ref>PMID:10945669</ref> Defects in FGFR2 are the cause of Beare-Stevenson cutis gyrata syndrome (BSCGS) [MIM:[https://omim.org/entry/123790 123790]]. BSCGS is an autosomal dominant condition is characterized by the furrowed skin disorder of cutis gyrata, acanthosis nigricans, craniosynostosis, craniofacial dysmorphism, digital anomalies, umbilical and anogenital abnormalities and early death.<ref>PMID:19387476</ref> <ref>PMID:8696350</ref> <ref>PMID:12000365</ref> Defects in FGFR2 are the cause of familial scaphocephaly syndrome (FSPC) [MIM:[https://omim.org/entry/609579 609579]]; also known as scaphocephaly with maxillary retrusion and mental retardation. FSPC is an autosomal dominant craniosynostosis syndrome characterized by scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion, and mild intellectual disability. Scaphocephaly is the most common of the craniosynostosis conditions and is characterized by a long, narrow head. It is due to premature fusion of the sagittal suture or from external deformation.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:16061565</ref> Defects in FGFR2 are a cause of lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:[https://omim.org/entry/149730 149730]]; also known as Levy-Hollister syndrome. LADDS is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. LADDS is an autosomal dominant syndrome characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed.<ref>PMID:19387476</ref> <ref>PMID:18056630</ref> <ref>PMID:16501574</ref> Defects in FGFR2 are the cause of Antley-Bixler syndrome without genital anomalies or disordered steroidogenesis (ABS2) [MIM:[https://omim.org/entry/207410 207410]]. A rare syndrome characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. Arachnodactyly and/or camptodactyly have also been reported.<ref>PMID:19387476</ref> <ref>PMID:10633130</ref> Defects in FGFR2 are the cause of Bent bone dysplasia syndrome (BBDS) [MIM:[https://omim.org/entry/614592 614592]]. BBDS is a perinatal lethal skeletal dysplasia characterized by poor mineralization of the calvarium, craniosynostosis, dysmorphic facial features, prenatal teeth, hypoplastic pubis and clavicles, osteopenia, and bent long bones. Dysmorphic facial features included low-set ears, hypertelorism, midface hypoplasia, prematurely erupted fetal teeth, and micrognathia.<ref>PMID:19387476</ref> <ref>PMID:22387015</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN]] Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1.<ref>PMID:8961926</ref> <ref>PMID:8663044</ref> <ref>PMID:12529371</ref> <ref>PMID:15190072</ref> <ref>PMID:15629145</ref> <ref>PMID:16597617</ref> <ref>PMID:16844695</ref> <ref>PMID:17623664</ref> <ref>PMID:17311277</ref> <ref>PMID:18374639</ref> <ref>PMID:19410646</ref> <ref>PMID:19103595</ref> <ref>PMID:21596750</ref> <ref>PMID:19387476</ref> <ref>PMID:16384934</ref>		[[https://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN]] Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1.<ref>PMID:8961926</ref> <ref>PMID:8663044</ref> <ref>PMID:12529371</ref> <ref>PMID:15190072</ref> <ref>PMID:15629145</ref> <ref>PMID:16597617</ref> <ref>PMID:16844695</ref> <ref>PMID:17623664</ref> <ref>PMID:17311277</ref> <ref>PMID:18374639</ref> <ref>PMID:19410646</ref> <ref>PMID:19103595</ref> <ref>PMID:21596750</ref> <ref>PMID:19387476</ref> <ref>PMID:16384934</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:

	==See Also==		==See Also==
	*[[Fibroblast growth factor receptor\|Fibroblast growth factor receptor]]		*[[Fibroblast growth factor receptor 3D receptor\|Fibroblast growth factor receptor 3D receptor]]
	== References ==		== References ==
	<references/>		<references/>
Line 41:		Line 41:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Receptor protein-tyrosine kinase]]		[[Category: Receptor protein-tyrosine kinase]]
	[[Category: Chen, H]]		[[Category: Chen, H]]

OCA at 09:08, 26 September 2018

2018-09-26T09:08:04Z

← Older revision		Revision as of 09:08, 26 September 2018
Line 3:		Line 3:
	<StructureSection load='2py3' size='340' side='right' caption='[[2py3]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2py3' size='340' side='right' caption='[[2py3]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2psq\|2psq]], [[2pvf\|2pvf]], [[2pvy\|2pvy]], [[2pwl\|2pwl]], [[2pz5\|2pz5]], [[2pzp\|2pzp]], [[2pzr\|2pzr]], [[2q0b\|2q0b]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2psq\|2psq]], [[2pvf\|2pvf]], [[2pvy\|2pvy]], [[2pwl\|2pwl]], [[2pz5\|2pz5]], [[2pzp\|2pzp]], [[2pzr\|2pzr]], [[2q0b\|2q0b]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FGFR2, BEK, KSAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [http://pdbe.org/2py3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [http://www.ebi.ac.uk/pdbsum/2py3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2py3 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [http://pdbe.org/2py3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [http://www.ebi.ac.uk/pdbsum/2py3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2py3 ProSAT]</span></td></tr>
Line 17:		Line 18:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/py/2py3_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/py/2py3_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 39:		Line 40:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
	[[Category: Receptor protein-tyrosine kinase]]		[[Category: Receptor protein-tyrosine kinase]]
	[[Category: Chen, H]]		[[Category: Chen, H]]

OCA at 14:42, 22 December 2016

2016-12-22T14:42:19Z

← Older revision		Revision as of 14:42, 22 December 2016
Line 1:		Line 1:
	==Crystal ~~Strucure~~ of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome==
			==Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome==
	<StructureSection load='2py3' size='340' side='right' caption='[[2py3]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2py3' size='340' side='right' caption='[[2py3]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Human Human]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2psq\|2psq]], [[2pvf\|2pvf]], [[2pvy\|2pvy]], [[2pwl\|2pwl]], [[2pz5\|2pz5]], [[2pzp\|2pzp]], [[2pzr\|2pzr]], [[2q0b\|2q0b]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2psq\|2psq]], [[2pvf\|2pvf]], [[2pvy\|2pvy]], [[2pwl\|2pwl]], [[2pz5\|2pz5]], [[2pzp\|2pzp]], [[2pzr\|2pzr]], [[2q0b\|2q0b]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FGFR2, BEK, KSAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [http://pdbe.org/2py3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [http://www.ebi.ac.uk/pdbsum/2py3 PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [http://pdbe.org/2py3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [http://www.ebi.ac.uk/pdbsum/2py3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2py3 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 39:		Line 39:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Human]]~~
	[[Category: Receptor protein-tyrosine kinase]]		[[Category: Receptor protein-tyrosine kinase]]
	[[Category: Chen, H]]		[[Category: Chen, H]]

OCA at 09:21, 9 February 2016

2016-02-09T09:21:38Z

← Older revision		Revision as of 09:21, 9 February 2016
Line 21:		Line 21:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2py3 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 20:50, 10 September 2015

2015-09-10T20:50:58Z

← Older revision		Revision as of 20:50, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2py3' size='340' side='right' caption='[[2py3]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2py3' size='340' side='right' caption='[[2py3]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2psq\|2psq]], [[2pvf\|2pvf]], [[2pvy\|2pvy]], [[2pwl\|2pwl]], [[2pz5\|2pz5]], [[2pzp\|2pzp]], [[2pzr\|2pzr]], [[2q0b\|2q0b]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2psq\|2psq]], [[2pvf\|2pvf]], [[2pvy\|2pvy]], [[2pwl\|2pwl]], [[2pz5\|2pz5]], [[2pzp\|2pzp]], [[2pzr\|2pzr]], [[2q0b\|2q0b]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FGFR2, BEK, KSAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FGFR2, BEK, KSAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [http://www.ebi.ac.uk/pdbsum/2py3 PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [http://pdbe.org/2py3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [http://www.ebi.ac.uk/pdbsum/2py3 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 31:		Line 31:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 2py3" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 39:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Receptor protein-tyrosine kinase]]		[[Category: Receptor protein-tyrosine kinase]]
	[[Category: Chen, H]]		[[Category: Chen, H]]

OCA at 16:32, 19 January 2015

2015-01-19T16:32:20Z

← Older revision		Revision as of 16:32, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2py3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PY3 FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2psq\|2psq]], [[2pvf\|2pvf]], [[2pvy\|2pvy]], [[2pwl\|2pwl]], [[2pz5\|2pz5]], [[2pzp\|2pzp]], [[2pzr\|2pzr]], [[2q0b\|2q0b]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2psq\|2psq]], [[2pvf\|2pvf]], [[2pvy\|2pvy]], [[2pwl\|2pwl]], [[2pz5\|2pz5]], [[2pzp\|2pzp]], [[2pzr\|2pzr]], [[2q0b\|2q0b]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FGFR2, BEK, KSAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FGFR2, BEK, KSAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [http://www.ebi.ac.uk/pdbsum/2py3 PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2py3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2py3 RCSB], [http://www.ebi.ac.uk/pdbsum/2py3 PDBsum]</span></td></tr>
	<table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN]] Defects in FGFR2 are the cause of Crouzon syndrome (CS) [MIM:[http://omim.org/entry/123500 123500]]; also called craniofacial dysostosis type I (CFD1). CS is an autosomal dominant syndrome characterized by craniosynostosis (premature fusion of the skull sutures), hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> [:]<ref>PMID:7581378</ref> <ref>PMID:7987400</ref> <ref>PMID:7874170</ref> <ref>PMID:7655462</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:8946174</ref> <ref>PMID:8956050</ref> <ref>PMID:9002682</ref> <ref>PMID:9152842</ref> <ref>PMID:9677057</ref> <ref>PMID:9521581</ref> <ref>PMID:10574673</ref> <ref>PMID:11173845</ref> <ref>PMID:11380921</ref> <ref>PMID:11781872</ref> Defects in FGFR2 are a cause of Jackson-Weiss syndrome (JWS) [MIM:[http://omim.org/entry/123150 123150]]. JWS is an autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence.<ref>PMID:19387476</ref> <ref>PMID:7874170</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:9677057</ref> <ref>PMID:9385368</ref> Defects in FGFR2 are a cause of Apert syndrome (APRS) [MIM:[http://omim.org/entry/101200 101200]]; also known as acrocephalosyndactyly type 1 (ACS1). APRS is a syndrome characterized by facio-cranio-synostosis, osseous and membranous syndactyly of the four extremities, and midface hypoplasia. The craniosynostosis is bicoronal and results in acrocephaly of brachysphenocephalic type. Syndactyly of the fingers and toes may be total (mitten hands and sock feet) or partial affecting the second, third, and fourth digits. Intellectual deficit is frequent and often severe, usually being associated with cerebral malformations.<ref>PMID:15190072</ref> <ref>PMID:19387476</ref> <ref>PMID:9002682</ref> <ref>PMID:9677057</ref> <ref>PMID:11781872</ref> <ref>PMID:7668257</ref> <ref>PMID:11390973</ref> <ref>PMID:7719344</ref> <ref>PMID:9452027</ref> Defects in FGFR2 are a cause of Pfeiffer syndrome (PS) [MIM:[http://omim.org/entry/101600 101600]]; also known as acrocephalosyndactyly type V (ACS5). PS is characterized by craniosynostosis (premature fusion of the skull sutures) with deviation and enlargement of the thumbs and great toes, brachymesophalangy, with phalangeal ankylosis and a varying degree of soft tissue syndactyly. Three subtypes of Pfeiffer syndrome have been described: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3).<ref>PMID:16844695</ref> <ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:8644708</ref> <ref>PMID:9002682</ref> <ref>PMID:11173845</ref> <ref>PMID:11781872</ref> <ref>PMID:7719333</ref> <ref>PMID:7719345</ref> <ref>PMID:9150725</ref> <ref>PMID:9693549</ref> <ref>PMID:9719378</ref> <ref>PMID:10394936</ref> <ref>PMID:10945669</ref> Defects in FGFR2 are the cause of Beare-Stevenson cutis gyrata syndrome (BSCGS) [MIM:[http://omim.org/entry/123790 123790]]. BSCGS is an autosomal dominant condition is characterized by the furrowed skin disorder of cutis gyrata, acanthosis nigricans, craniosynostosis, craniofacial dysmorphism, digital anomalies, umbilical and anogenital abnormalities and early death.<ref>PMID:19387476</ref> <ref>PMID:8696350</ref> <ref>PMID:12000365</ref> Defects in FGFR2 are the cause of familial scaphocephaly syndrome (FSPC) [MIM:[http://omim.org/entry/609579 609579]]; also known as scaphocephaly with maxillary retrusion and mental retardation. FSPC is an autosomal dominant craniosynostosis syndrome characterized by scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion, and mild intellectual disability. Scaphocephaly is the most common of the craniosynostosis conditions and is characterized by a long, narrow head. It is due to premature fusion of the sagittal suture or from external deformation.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:16061565</ref> Defects in FGFR2 are a cause of lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:[http://omim.org/entry/149730 149730]]; also known as Levy-Hollister syndrome. LADDS is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. LADDS is an autosomal dominant syndrome characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed.<ref>PMID:19387476</ref> <ref>PMID:18056630</ref> <ref>PMID:16501574</ref> Defects in FGFR2 are the cause of Antley-Bixler syndrome without genital anomalies or disordered steroidogenesis (ABS2) [MIM:[http://omim.org/entry/207410 207410]]. A rare syndrome characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. Arachnodactyly and/or camptodactyly have also been reported.<ref>PMID:19387476</ref> <ref>PMID:10633130</ref> Defects in FGFR2 are the cause of Bent bone dysplasia syndrome (BBDS) [MIM:[http://omim.org/entry/614592 614592]]. BBDS is a perinatal lethal skeletal dysplasia characterized by poor mineralization of the calvarium, craniosynostosis, dysmorphic facial features, prenatal teeth, hypoplastic pubis and clavicles, osteopenia, and bent long bones. Dysmorphic facial features included low-set ears, hypertelorism, midface hypoplasia, prematurely erupted fetal teeth, and micrognathia.<ref>PMID:19387476</ref> <ref>PMID:22387015</ref>		[[http://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN]] Defects in FGFR2 are the cause of Crouzon syndrome (CS) [MIM:[http://omim.org/entry/123500 123500]]; also called craniofacial dysostosis type I (CFD1). CS is an autosomal dominant syndrome characterized by craniosynostosis (premature fusion of the skull sutures), hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> [:]<ref>PMID:7581378</ref> <ref>PMID:7987400</ref> <ref>PMID:7874170</ref> <ref>PMID:7655462</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:8946174</ref> <ref>PMID:8956050</ref> <ref>PMID:9002682</ref> <ref>PMID:9152842</ref> <ref>PMID:9677057</ref> <ref>PMID:9521581</ref> <ref>PMID:10574673</ref> <ref>PMID:11173845</ref> <ref>PMID:11380921</ref> <ref>PMID:11781872</ref> Defects in FGFR2 are a cause of Jackson-Weiss syndrome (JWS) [MIM:[http://omim.org/entry/123150 123150]]. JWS is an autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence.<ref>PMID:19387476</ref> <ref>PMID:7874170</ref> <ref>PMID:8528214</ref> <ref>PMID:8644708</ref> <ref>PMID:9677057</ref> <ref>PMID:9385368</ref> Defects in FGFR2 are a cause of Apert syndrome (APRS) [MIM:[http://omim.org/entry/101200 101200]]; also known as acrocephalosyndactyly type 1 (ACS1). APRS is a syndrome characterized by facio-cranio-synostosis, osseous and membranous syndactyly of the four extremities, and midface hypoplasia. The craniosynostosis is bicoronal and results in acrocephaly of brachysphenocephalic type. Syndactyly of the fingers and toes may be total (mitten hands and sock feet) or partial affecting the second, third, and fourth digits. Intellectual deficit is frequent and often severe, usually being associated with cerebral malformations.<ref>PMID:15190072</ref> <ref>PMID:19387476</ref> <ref>PMID:9002682</ref> <ref>PMID:9677057</ref> <ref>PMID:11781872</ref> <ref>PMID:7668257</ref> <ref>PMID:11390973</ref> <ref>PMID:7719344</ref> <ref>PMID:9452027</ref> Defects in FGFR2 are a cause of Pfeiffer syndrome (PS) [MIM:[http://omim.org/entry/101600 101600]]; also known as acrocephalosyndactyly type V (ACS5). PS is characterized by craniosynostosis (premature fusion of the skull sutures) with deviation and enlargement of the thumbs and great toes, brachymesophalangy, with phalangeal ankylosis and a varying degree of soft tissue syndactyly. Three subtypes of Pfeiffer syndrome have been described: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3).<ref>PMID:16844695</ref> <ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:8644708</ref> <ref>PMID:9002682</ref> <ref>PMID:11173845</ref> <ref>PMID:11781872</ref> <ref>PMID:7719333</ref> <ref>PMID:7719345</ref> <ref>PMID:9150725</ref> <ref>PMID:9693549</ref> <ref>PMID:9719378</ref> <ref>PMID:10394936</ref> <ref>PMID:10945669</ref> Defects in FGFR2 are the cause of Beare-Stevenson cutis gyrata syndrome (BSCGS) [MIM:[http://omim.org/entry/123790 123790]]. BSCGS is an autosomal dominant condition is characterized by the furrowed skin disorder of cutis gyrata, acanthosis nigricans, craniosynostosis, craniofacial dysmorphism, digital anomalies, umbilical and anogenital abnormalities and early death.<ref>PMID:19387476</ref> <ref>PMID:8696350</ref> <ref>PMID:12000365</ref> Defects in FGFR2 are the cause of familial scaphocephaly syndrome (FSPC) [MIM:[http://omim.org/entry/609579 609579]]; also known as scaphocephaly with maxillary retrusion and mental retardation. FSPC is an autosomal dominant craniosynostosis syndrome characterized by scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion, and mild intellectual disability. Scaphocephaly is the most common of the craniosynostosis conditions and is characterized by a long, narrow head. It is due to premature fusion of the sagittal suture or from external deformation.<ref>PMID:19387476</ref> <ref>PMID:17803937</ref> <ref>PMID:16061565</ref> Defects in FGFR2 are a cause of lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:[http://omim.org/entry/149730 149730]]; also known as Levy-Hollister syndrome. LADDS is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. LADDS is an autosomal dominant syndrome characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed.<ref>PMID:19387476</ref> <ref>PMID:18056630</ref> <ref>PMID:16501574</ref> Defects in FGFR2 are the cause of Antley-Bixler syndrome without genital anomalies or disordered steroidogenesis (ABS2) [MIM:[http://omim.org/entry/207410 207410]]. A rare syndrome characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. Arachnodactyly and/or camptodactyly have also been reported.<ref>PMID:19387476</ref> <ref>PMID:10633130</ref> Defects in FGFR2 are the cause of Bent bone dysplasia syndrome (BBDS) [MIM:[http://omim.org/entry/614592 614592]]. BBDS is a perinatal lethal skeletal dysplasia characterized by poor mineralization of the calvarium, craniosynostosis, dysmorphic facial features, prenatal teeth, hypoplastic pubis and clavicles, osteopenia, and bent long bones. Dysmorphic facial features included low-set ears, hypertelorism, midface hypoplasia, prematurely erupted fetal teeth, and micrognathia.<ref>PMID:19387476</ref> <ref>PMID:22387015</ref>
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	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Receptor protein-tyrosine kinase]]		[[Category: Receptor protein-tyrosine kinase]]
	[[Category: Chen, H.]]		[[Category: Chen, H]]
	[[Category: Mohammadi, M.]]		[[Category: Mohammadi, M]]
	[[Category: Kinase domain fold consisting of n- and c-lobe]]		[[Category: Kinase domain fold consisting of n- and c-lobe]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 19:19, 30 September 2014

2014-09-30T19:19:26Z

Show changes

OCA at 05:36, 25 March 2013

2013-03-25T05:36:50Z

← Older revision		Revision as of 05:36, 25 March 2013
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	~~[[Image:2py3.png\|left\|200px]]~~

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2py3", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
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	{{STRUCTURE_2py3\| PDB=2py3 \| SCENE= }}		{{STRUCTURE_2py3\| PDB=2py3 \| SCENE= }}

	===Crystal Strucure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome===		===Crystal Strucure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic E565G Mutation Responsible for Pfeiffer Syndrome===
			{{ABSTRACT_PUBMED_17803937}}

			==Disease==
			[[http://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN]] Defects in FGFR2 are the cause of Crouzon syndrome (CS) [MIM:[http://omim.org/entry/123500 123500]]; also called craniofacial dysostosis type I (CFD1). CS is an autosomal dominant syndrome characterized by craniosynostosis (premature fusion of the skull sutures), hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism.<ref>PMID:19387476</ref><ref>PMID:17803937</ref>[:]<ref>PMID:7581378</ref><ref>PMID:7987400</ref><ref>PMID:7874170</ref><ref>PMID:7655462</ref><ref>PMID:8528214</ref><ref>PMID:8644708</ref><ref>PMID:8946174</ref><ref>PMID:8956050</ref><ref>PMID:9002682</ref><ref>PMID:9152842</ref><ref>PMID:9677057</ref><ref>PMID:9521581</ref><ref>PMID:10574673</ref><ref>PMID:11173845</ref><ref>PMID:11380921</ref><ref>PMID:11781872</ref> Defects in FGFR2 are a cause of Jackson-Weiss syndrome (JWS) [MIM:[http://omim.org/entry/123150 123150]]. JWS is an autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence.<ref>PMID:19387476</ref><ref>PMID:7874170</ref><ref>PMID:8528214</ref><ref>PMID:8644708</ref><ref>PMID:9677057</ref><ref>PMID:9385368</ref> Defects in FGFR2 are a cause of Apert syndrome (APRS) [MIM:[http://omim.org/entry/101200 101200]]; also known as acrocephalosyndactyly type 1 (ACS1). APRS is a syndrome characterized by facio-cranio-synostosis, osseous and membranous syndactyly of the four extremities, and midface hypoplasia. The craniosynostosis is bicoronal and results in acrocephaly of brachysphenocephalic type. Syndactyly of the fingers and toes may be total (mitten hands and sock feet) or partial affecting the second, third, and fourth digits. Intellectual deficit is frequent and often severe, usually being associated with cerebral malformations.<ref>PMID:15190072</ref><ref>PMID:19387476</ref><ref>PMID:9002682</ref><ref>PMID:9677057</ref><ref>PMID:11781872</ref><ref>PMID:7668257</ref><ref>PMID:11390973</ref><ref>PMID:7719344</ref><ref>PMID:9452027</ref> Defects in FGFR2 are a cause of Pfeiffer syndrome (PS) [MIM:[http://omim.org/entry/101600 101600]]; also known as acrocephalosyndactyly type V (ACS5). PS is characterized by craniosynostosis (premature fusion of the skull sutures) with deviation and enlargement of the thumbs and great toes, brachymesophalangy, with phalangeal ankylosis and a varying degree of soft tissue syndactyly. Three subtypes of Pfeiffer syndrome have been described: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3).<ref>PMID:16844695</ref><ref>PMID:19387476</ref><ref>PMID:17803937</ref><ref>PMID:8644708</ref><ref>PMID:9002682</ref><ref>PMID:11173845</ref><ref>PMID:11781872</ref><ref>PMID:7719333</ref><ref>PMID:7719345</ref><ref>PMID:9150725</ref><ref>PMID:9693549</ref><ref>PMID:9719378</ref><ref>PMID:10394936</ref><ref>PMID:10945669</ref> Defects in FGFR2 are the cause of Beare-Stevenson cutis gyrata syndrome (BSCGS) [MIM:[http://omim.org/entry/123790 123790]]. BSCGS is an autosomal dominant condition is characterized by the furrowed skin disorder of cutis gyrata, acanthosis nigricans, craniosynostosis, craniofacial dysmorphism, digital anomalies, umbilical and anogenital abnormalities and early death.<ref>PMID:19387476</ref><ref>PMID:8696350</ref><ref>PMID:12000365</ref> Defects in FGFR2 are the cause of familial scaphocephaly syndrome (FSPC) [MIM:[http://omim.org/entry/609579 609579]]; also known as scaphocephaly with maxillary retrusion and mental retardation. FSPC is an autosomal dominant craniosynostosis syndrome characterized by scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion, and mild intellectual disability. Scaphocephaly is the most common of the craniosynostosis conditions and is characterized by a long, narrow head. It is due to premature fusion of the sagittal suture or from external deformation.<ref>PMID:19387476</ref><ref>PMID:17803937</ref><ref>PMID:16061565</ref> Defects in FGFR2 are a cause of lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:[http://omim.org/entry/149730 149730]]; also known as Levy-Hollister syndrome. LADDS is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. LADDS is an autosomal dominant syndrome characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed.<ref>PMID:19387476</ref><ref>PMID:18056630</ref><ref>PMID:16501574</ref> Defects in FGFR2 are the cause of Antley-Bixler syndrome without genital anomalies or disordered steroidogenesis (ABS2) [MIM:[http://omim.org/entry/207410 207410]]. A rare syndrome characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. Arachnodactyly and/or camptodactyly have also been reported.<ref>PMID:19387476</ref><ref>PMID:10633130</ref> Defects in FGFR2 are the cause of Bent bone dysplasia syndrome (BBDS) [MIM:[http://omim.org/entry/614592 614592]]. BBDS is a perinatal lethal skeletal dysplasia characterized by poor mineralization of the calvarium, craniosynostosis, dysmorphic facial features, prenatal teeth, hypoplastic pubis and clavicles, osteopenia, and bent long bones. Dysmorphic facial features included low-set ears, hypertelorism, midface hypoplasia, prematurely erupted fetal teeth, and micrognathia.<ref>PMID:19387476</ref><ref>PMID:22387015</ref>

	<!--		==Function==
	~~The line below this paragraph~~, ~~{{ABSTRACT_PUBMED_17803937}}~~, ~~adds~~ the ~~Publication Abstract~~ to the ~~page~~		[[http://www.uniprot.org/uniprot/FGFR2_HUMAN FGFR2_HUMAN]] Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1.<ref>PMID:8961926</ref><ref>PMID:8663044</ref><ref>PMID:12529371</ref><ref>PMID:15190072</ref><ref>PMID:15629145</ref><ref>PMID:16597617</ref><ref>PMID:16844695</ref><ref>PMID:17623664</ref><ref>PMID:17311277</ref><ref>PMID:18374639</ref><ref>PMID:19410646</ref><ref>PMID:19103595</ref><ref>PMID:21596750</ref><ref>PMID:19387476</ref><ref>PMID:16384934</ref>
	~~(as it appears on PubMed at http:~~//~~www~~.~~pubmed~~.~~gov)~~, ~~where 17803937 is the PubMed ID number~~.
	-->
	~~{{ABSTRACT_PUBMED_17803937}}~~

	==About this Structure==		==About this Structure==
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	==Reference==		==Reference==
	<ref group="xtra">PMID:017803937</ref><references group="xtra"/>		<ref group="xtra">PMID:017803937</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Receptor protein-tyrosine kinase]]		[[Category: Receptor protein-tyrosine kinase]]

OCA: Protected "2py3" [edit=sysop:move=sysop]

2012-03-08T04:52:15Z

Protected "2py3" [edit=sysop:move=sysop]

← Older revision	Revision as of 04:52, 8 March 2012
(No difference)