From Wikipedia, the free encyclopedia
GAF domain
3',5'-Cyclic Nucleotide Phosphodiesterase 2A, Containing the GAF A and GAF B Domains. [1]
Identifiers
SymbolGAF
Pfam PF01590
Pfam clan CL0161
InterPro IPR003018
SMART GAF
SCOP2 1fl4 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

The GAF domain is a type of protein domain that is found in a wide range of proteins from all species. [2] The GAF domain is named after some of the proteins it is found in: cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. The first structure of a GAF domain solved by Ho and colleagues showed that this domain shared a similar fold with the PAS domain. [3] In mammals, GAF domains are found in five members of the cyclic nucleotide phosphodiesterase superfamily: PDE2, PDE5, and PDE6 which bind cGMP to the GAF domain, PDE10 which binds cAMP, and PDE11 which binds both cGMP and cAMP. [4] [5]

Examples

Human proteins containing this domain include:

References

  1. ^ Martinez SE, Wu AY, Glavas NA, Tang XB, Turley S, Hol WG, Beavo JA (October 2002). "The two GAF domains in phosphodiesterase 2A have distinct roles in dimerization and in cGMP binding". Proceedings of the National Academy of Sciences of the United States of America. 99 (20): 13260–5. Bibcode: 2002PNAS...9913260M. doi: 10.1073/pnas.192374899. JSTOR  3073384. PMC  130621. PMID  12271124.
  2. ^ Aravind L, Ponting CP (December 1997). "The GAF domain: an evolutionary link between diverse phototransducing proteins". Trends in Biochemical Sciences. 22 (12): 458–9. doi: 10.1016/S0968-0004(97)01148-1. PMID  9433123.
  3. ^ Ho YS, Burden LM, Hurley JH (October 2000). "Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor". The EMBO Journal. 19 (20): 5288–99. doi: 10.1093/emboj/19.20.5288. PMC  314001. PMID  11032796.
  4. ^ Fawcett L, Baxendale R, Stacey P, McGrouther C, Harrow I, Soderling S, Hetman J, Beavo JA, Phillips SC (March 2000). "Molecular cloning and characterization of a distinct human phosphodiesterase gene family: PDE11A". Proceedings of the National Academy of Sciences of the United States of America. 97 (7): 3702–7. Bibcode: 2000PNAS...97.3702F. doi: 10.1073/pnas.050585197. JSTOR  121956. PMC  16303. PMID  10725373.
  5. ^ Schultz JE (2009). "Structural and biochemical aspects of tandem GAF domains". CGMP: Generators, Effectors and Therapeutic Implications. Handbook of Experimental Pharmacology. Vol. 191. pp. 93–109. doi: 10.1007/978-3-540-68964-5_6. ISBN  978-3-540-68960-7. PMID  19089327.
From Wikipedia, the free encyclopedia
GAF domain
3',5'-Cyclic Nucleotide Phosphodiesterase 2A, Containing the GAF A and GAF B Domains. [1]
Identifiers
SymbolGAF
Pfam PF01590
Pfam clan CL0161
InterPro IPR003018
SMART GAF
SCOP2 1fl4 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

The GAF domain is a type of protein domain that is found in a wide range of proteins from all species. [2] The GAF domain is named after some of the proteins it is found in: cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. The first structure of a GAF domain solved by Ho and colleagues showed that this domain shared a similar fold with the PAS domain. [3] In mammals, GAF domains are found in five members of the cyclic nucleotide phosphodiesterase superfamily: PDE2, PDE5, and PDE6 which bind cGMP to the GAF domain, PDE10 which binds cAMP, and PDE11 which binds both cGMP and cAMP. [4] [5]

Examples

Human proteins containing this domain include:

References

  1. ^ Martinez SE, Wu AY, Glavas NA, Tang XB, Turley S, Hol WG, Beavo JA (October 2002). "The two GAF domains in phosphodiesterase 2A have distinct roles in dimerization and in cGMP binding". Proceedings of the National Academy of Sciences of the United States of America. 99 (20): 13260–5. Bibcode: 2002PNAS...9913260M. doi: 10.1073/pnas.192374899. JSTOR  3073384. PMC  130621. PMID  12271124.
  2. ^ Aravind L, Ponting CP (December 1997). "The GAF domain: an evolutionary link between diverse phototransducing proteins". Trends in Biochemical Sciences. 22 (12): 458–9. doi: 10.1016/S0968-0004(97)01148-1. PMID  9433123.
  3. ^ Ho YS, Burden LM, Hurley JH (October 2000). "Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor". The EMBO Journal. 19 (20): 5288–99. doi: 10.1093/emboj/19.20.5288. PMC  314001. PMID  11032796.
  4. ^ Fawcett L, Baxendale R, Stacey P, McGrouther C, Harrow I, Soderling S, Hetman J, Beavo JA, Phillips SC (March 2000). "Molecular cloning and characterization of a distinct human phosphodiesterase gene family: PDE11A". Proceedings of the National Academy of Sciences of the United States of America. 97 (7): 3702–7. Bibcode: 2000PNAS...97.3702F. doi: 10.1073/pnas.050585197. JSTOR  121956. PMC  16303. PMID  10725373.
  5. ^ Schultz JE (2009). "Structural and biochemical aspects of tandem GAF domains". CGMP: Generators, Effectors and Therapeutic Implications. Handbook of Experimental Pharmacology. Vol. 191. pp. 93–109. doi: 10.1007/978-3-540-68964-5_6. ISBN  978-3-540-68960-7. PMID  19089327.

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