Growth factor receptor-bound protein: Difference between revisions

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<StructureSection load='1tze' size='350' side='right' caption='Structure of human Grb2 SH2 domain (pink) complex with phosphotyrosyl heptapeptide (gold)  (PDB entry [[1tze]])' scene=''>
<StructureSection load='' size='350' side='right' caption='Structure of human Grb2 SH2 domain (green) complex with phosphotyrosyl polypeptide (magenta)  (PDB entry [[1bmb]])' scene='51/516448/Cv/1'>
== Function ==
'''Growth factor receptor-bound proteins''' (GRB) are adaptor proteins.  GRBs contain SH2, Ras-associated (RA) and pleckstrin homology (PH) domains. <br />
'''Growth factor receptor-bound proteins''' (GRB) are adaptor proteins.  GRBs contain SH2, Ras-associated (RA) and pleckstrin homology (PH) domains. <br />
*  '''GRB2''' links the epidermal growth factor receptor tyrosine kinase to the activation of Ras and its downstream kinases.  GRB2 contains an SH2 domain which binds tyrosine phosphorylated sequences and 2 SH3 domains which direct complex formation of proline-rich sequences.  GRB2 is involved in signal transduction.<br />
*  '''GRB2''' links the epidermal growth factor receptor tyrosine kinase to the activation of Ras and its downstream kinases.  GRB2 contains an SH2 domain which binds tyrosine phosphorylated sequences and 2 SH3 domains which direct complex formation of proline-rich sequences.  GRB2 is involved in signal transduction<ref>PMID:1322798</ref>.<br />
*  '''GRB7''' interacts with EGFR and ephrin receptors and plays a role in itegrin signalling pathway.<br />
*  '''GRB7''' interacts with EGFR and ephrin receptors and plays a role in itegrin signalling pathway<ref>PMID:19717535</ref>.<br />
*  '''GRB10''' interacts with insulin receptor and insulin-like growth factor receptors.  For additional details on GRB10 see [[Grb10 SH2 Domain]].<br />
*  '''GRB10''' and '''GRB14''' interact with insulin receptor and insulin-like growth factor receptors<ref>PMID:12783867</ref>.  For additional details on GRB10 see [[Grb10 SH2 Domain]].<br />


==3D structures of Grb==
== Structural highlights ==
Human GRB2 residue <scene name='51/516448/Cv/5'>Trp121 forces the phosphotyrosyl containing ligand</scene> into a turn conformation. Water molecules are shown as red spheres. <scene name='51/516448/Cv/6'>Phosphotyrosine binding</scene>  <ref>PMID:10090780</ref>.


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
==3D structures of growth factor receptor-bound proteins==
{{#tree:id=OrganizedByTopic|openlevels=0|
[[Growth factor receptor-bound proteins 3D structures]]


*GRB2
</StructureSection>


**[[1gri]], [[2h46]] – hGRB2 – human <br />
== References ==
 
<references/>
*''GRB2 C terminal SH3 domain''
 
**[[1gfc]], [[1gfd]] – hGRB2 C terminal SH3 domain - NMR<br />
**[[2vvk]], [[2vwf]], [[2w0z]] – hGRB2 C terminal SH3 domain <br />
**[[1io6]] – hGRB2 C terminal SH3 domain + ligand peptide - NMR<br />
**[[1gcq]] – hGRB2 C terminal SH3 domain + VAV proto-oncogene SH3 domain<br />
 
*''GRB2 N terminal SH3 domain''
 
**[[1gbr]], [[1gbq]], [[2gbq]], [[3gbq]], [[4gbq]] – mGRB2 N terminal SH3 domain + Sos-A peptide – mouse - NMR<br />
**[[1aze]] – mGRB2 N terminal SH3 domain + Sos-A peptide - NMR<br />
 
*''GRB2 SH2 domain''
 
**[[1jyu]] – hGRB2 SH2 domain <br />
**[[1ghu]] – hGRB2 SH2 domain (mutant) - NMR<br />
**[[1fhs]] – hGRB2 SH2 domain - NMR<br />
**[[1x0n]] – hGRB2 SH2 domain + inhibitor - NMR<br />
**[[2huw]] – hGRB2 SH2 domain + cyclopropane derivative<br />
**[[1cj1]] – hGRB2 SH2 domain + phosphor-Tyr derivative<br />
**[[2aoa]], [[2aob]] – hGRB2 SH2 domain + peptide mimetic<br />
**[[1tze]], [[1bmb]], [[1bm2]], [[1zfp]], [[1fyr]], [[1jyq]], [[1jyr]], [[2h5k]], [[3c7i]], [[3imd]], [[3imj]], [[3in7]], [[3in8]], [[3kfj]], [[3n8m]], [[3n7y]], [[3n84]], [[3mxc]], [[3mxy]], [[3ov1]], [[3ove]], [[3s8l]], [[3s8n]], [[3s8o]], [[1zfp]] – hGRB2 SH2 domain + phosphor-Tyr peptide<br />
**[[1qg1]] – hGRB2 SH2 domain + phosphor-Tyr peptide - NMR<br />
**[[3wa4]] - hGRB2 SH2 domain + CD28 peptide <br />
 
*GRB4
 
**[[4e6r]] – hGRB4 C terminal SH3 domain <br />
 
*GRB7
 
**[[2qms]] – hGRB7 SH2 domain <br />
**[[1mw4]], [[2l4k]] – hGRB7 SH2 domain + phosphor-Tyr peptide - NMR<br />
**[[3pqz]] – hGRB7 SH2 domain + cyclic peptide <br />
**[[1wgr]] – hGRB7 RA domain - NMR<br />
 
*GRB10
 
**[[1nrv]] – hGRB10 SH2 domain <br />
**[[3m7f]] – hGRB10 SH2 domain + NEDD4 C2 domain<br />
**[[3hk0]] – hGRB10 RA and PH domains <br />
 
*GRB14
 
**[[2aug]] – hGRB14 SH2 domain <br />
**[[2auh]] – hGRB14 BPS domain + insulin receptor kinase domain<br />
**[[4k81]] – hGRB14 RA and PH domains + GTPase Hras<br />
}}
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 10:53, 18 July 2019

Function

Growth factor receptor-bound proteins (GRB) are adaptor proteins. GRBs contain SH2, Ras-associated (RA) and pleckstrin homology (PH) domains.

  • GRB2 links the epidermal growth factor receptor tyrosine kinase to the activation of Ras and its downstream kinases. GRB2 contains an SH2 domain which binds tyrosine phosphorylated sequences and 2 SH3 domains which direct complex formation of proline-rich sequences. GRB2 is involved in signal transduction[1].
  • GRB7 interacts with EGFR and ephrin receptors and plays a role in itegrin signalling pathway[2].
  • GRB10 and GRB14 interact with insulin receptor and insulin-like growth factor receptors[3]. For additional details on GRB10 see Grb10 SH2 Domain.

Structural highlights

Human GRB2 residue into a turn conformation. Water molecules are shown as red spheres. [4].

3D structures of growth factor receptor-bound proteins

Growth factor receptor-bound proteins 3D structures


Structure of human Grb2 SH2 domain (green) complex with phosphotyrosyl polypeptide (magenta) (PDB entry 1bmb)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Lowenstein EJ, Daly RJ, Batzer AG, Li W, Margolis B, Lammers R, Ullrich A, Skolnik EY, Bar-Sagi D, Schlessinger J. The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling. Cell. 1992 Aug 7;70(3):431-42. PMID:1322798
  2. ↑ Nadler Y, Gonzalez AM, Camp RL, Rimm DL, Kluger HM, Kluger Y. Growth factor receptor-bound protein-7 (Grb7) as a prognostic marker and therapeutic target in breast cancer. Ann Oncol. 2010 Mar;21(3):466-73. doi: 10.1093/annonc/mdp346. Epub 2009 Aug 28. PMID:19717535 doi:http://dx.doi.org/10.1093/annonc/mdp346
  3. ↑ Deng Y, Bhattacharya S, Swamy OR, Tandon R, Wang Y, Janda R, Riedel H. Growth factor receptor-binding protein 10 (Grb10) as a partner of phosphatidylinositol 3-kinase in metabolic insulin action. J Biol Chem. 2003 Oct 10;278(41):39311-22. Epub 2003 Jun 3. PMID:12783867 doi:http://dx.doi.org/10.1074/jbc.M304599200
  4. ↑ Ettmayer P, France D, Gounarides J, Jarosinski M, Martin MS, Rondeau JM, Sabio M, Topiol S, Weidmann B, Zurini M, Bair KW. Structural and conformational requirements for high-affinity binding to the SH2 domain of Grb2(1). J Med Chem. 1999 Mar 25;42(6):971-80. PMID:10090780 doi:10.1021/jm9811007

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Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman
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