2pvf: Difference between revisions

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[[Image:2pvf.jpg|left|200px]]<br /><applet load="2pvf" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2pvf.jpg|left|200px]]
caption="2pvf, resolution 1.8&Aring;" />
 
'''Crystal Structure of Tyrosine Phosphorylated Activated FGF Receptor 2 (FGFR2) Kinase Domain in Complex with ATP Analog and Substrate Peptide'''<br />
{{Structure
|PDB= 2pvf |SIZE=350|CAPTION= <scene name='initialview01'>2pvf</scene>, resolution 1.8&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ABG:ADENOSINE 5'-[BETA,GAMMA-METHYLENE]TRIPHOSPHATE'>ABG</scene>
|ACTIVITY= [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]
|GENE= FGFR2, BEK, KSAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''Crystal Structure of Tyrosine Phosphorylated Activated FGF Receptor 2 (FGFR2) Kinase Domain in Complex with ATP Analog and Substrate Peptide'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2PVF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ABG:'>ABG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVF OCA].  
2PVF is a [[Protein complex]] structure of sequences 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=2PVF OCA].  


==Reference==
==Reference==
A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases., Chen H, Ma J, Li W, Eliseenkova AV, Xu C, Neubert TA, Miller WT, Mohammadi M, Mol Cell. 2007 Sep 7;27(5):717-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17803937 17803937]
A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases., Chen H, Ma J, Li W, Eliseenkova AV, Xu C, Neubert TA, Miller WT, Mohammadi M, Mol Cell. 2007 Sep 7;27(5):717-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17803937 17803937]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: ABG]]
[[Category: ABG]]
[[Category: MG]]
[[Category: MG]]
[[Category: kinase domain fold consisting of n- and c-lobes]]
[[Category: kinase domain fold consisting of n- and c-lobe]]
[[Category: transferase]]
[[Category: transferase]]


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Revision as of 19:17, 20 March 2008

File:2pvf.jpg


PDB ID 2pvf

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: and
Gene: FGFR2, BEK, KSAM (Homo sapiens)
Activity: Receptor protein-tyrosine kinase, with EC number 2.7.10.1
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Tyrosine Phosphorylated Activated FGF Receptor 2 (FGFR2) Kinase Domain in Complex with ATP Analog and Substrate Peptide


OverviewOverview

Activating mutations in the tyrosine kinase domain of receptor tyrosine kinases (RTKs) cause cancer and skeletal disorders. Comparison of the crystal structures of unphosphorylated and phosphorylated wild-type FGFR2 kinase domains with those of seven unphosphorylated pathogenic mutants reveals an autoinhibitory "molecular brake" mediated by a triad of residues in the kinase hinge region of all FGFRs. Structural analysis shows that many other RTKs, including PDGFRs, VEGFRs, KIT, CSF1R, FLT3, TEK, and TIE, are also subject to regulation by this brake. Pathogenic mutations activate FGFRs and other RTKs by disengaging the brake either directly or indirectly.

DiseaseDisease

Known diseases associated with this structure: Antley-Bixler syndrome, 207410 ( OMIM:[176943], Apert syndrome OMIM:[176943], Beare-Stevenson cutis gyrata syndrome OMIM:[176943], Craniofacial-skeletal-dermatologic dysplasia OMIM:[176943], Craniosynostosis, nonspecific OMIM:[176943], Crouzon syndrome OMIM:[176943], Gastric cancer, somatic OMIM:[176943], Jackson-Weiss syndrome OMIM:[176943], Pfeiffer syndrome OMIM:[176943], Saethre-Chotzen syndrome OMIM:[176943]

About this StructureAbout this Structure

2PVF is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases., Chen H, Ma J, Li W, Eliseenkova AV, Xu C, Neubert TA, Miller WT, Mohammadi M, Mol Cell. 2007 Sep 7;27(5):717-30. PMID:17803937

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