Growth factor receptor-bound protein: Difference between revisions

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== Structural highlights ==
== 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>.
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>.
==3D structures of growth factor receptor-bound proteins==
[[Growth factor receptor-bound proteins 3D structures]]
</StructureSection>
</StructureSection>


Line 19: Line 23:
**[[1gri]], [[2h46]] – hGRB2 – human <br />
**[[1gri]], [[2h46]] – hGRB2 – human <br />


*''GRB2 C terminal SH3 domain''
*''GRB2 C terminal SH3 domain'' residues 159-214


**[[1gfc]], [[1gfd]] – hGRB2 C terminal SH3 domain - NMR<br />
**[[1gfc]], [[1gfd]] – hGRB2 C terminal SH3 domain - NMR<br />
Line 26: Line 30:
**[[1gcq]] – hGRB2 C terminal SH3 domain + VAV proto-oncogene SH3 domain<br />
**[[1gcq]] – hGRB2 C terminal SH3 domain + VAV proto-oncogene SH3 domain<br />


*''GRB2 N terminal SH3 domain''
*''GRB2 N terminal SH3 domain'' residues 1-61


**[[1gbr]], [[1gbq]], [[2gbq]], [[3gbq]], [[4gbq]] – mGRB2 N terminal SH3 domain + Sos-A peptide – mouse - NMR<br />
**[[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 />
**[[1aze]] – mGRB2 N terminal SH3 domain + Sos-A peptide - NMR<br />


*''GRB2 SH2 domain''
*''GRB2 SH2 domain'' residues 60-158


**[[1jyu]] – hGRB2 SH2 domain <br />
**[[1jyu]], [[6icg]], [[6ich]] – hGRB2 SH2 domain <br />
**[[1ghu]] – hGRB2 SH2 domain (mutant) - NMR<br />
**[[1ghu]] – hGRB2 SH2 domain (mutant) - NMR<br />
**[[1fhs]] – hGRB2 SH2 domain - NMR<br />
**[[1fhs]] – hGRB2 SH2 domain - NMR<br />
Line 55: Line 59:
**[[1mw4]], [[2l4k]] – hGRB7 SH2 domain + phosphor-Tyr peptide - NMR<br />
**[[1mw4]], [[2l4k]] – hGRB7 SH2 domain + phosphor-Tyr peptide - NMR<br />
**[[3pqz]], [[5u1q]], [[5u06]], [[5tyi]] – hGRB7 SH2 domain + cyclic peptide <br />
**[[3pqz]], [[5u1q]], [[5u06]], [[5tyi]] – hGRB7 SH2 domain + cyclic peptide <br />
**[[1wgr]] – hGRB7 RA domain - NMR<br />
**[[1wgr]] – hGRB7 RA domain residues 100-186 - NMR<br />


*GRB10
*GRB10
Line 61: Line 65:
**[[1nrv]] – hGRB10 SH2 domain <br />
**[[1nrv]] – hGRB10 SH2 domain <br />
**[[3m7f]] – hGRB10 SH2 domain + NEDD4 C2 domain<br />
**[[3m7f]] – hGRB10 SH2 domain + NEDD4 C2 domain<br />
**[[3hk0]] – hGRB10 RA and PH domains <br />
**[[3hk0]] – hGRB10 PH domain residues 164-415 <br />


*GRB14
*GRB14

Revision as of 10:52, 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

3D structures of growth factor receptor-bound proteins3D structures of growth factor receptor-bound proteins

Updated on 18-July-2019

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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