Biology:GAF domain

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GAF domain
PDB 1mc0 EBI.jpg
3',5'-Cyclic Nucleotide Phosphodiesterase 2A, Containing the GAF A and GAF B Domains.[1]
Identifiers
SymbolGAF
PfamPF01590
Pfam clanCL0161
InterProIPR003018
SMARTGAF
SCOP21fl4 / SCOPe / SUPFAM

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. "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. October 2002. doi:10.1073/pnas.192374899. PMID 12271124. Bibcode2002PNAS...9913260M. 
  2. "The GAF domain: an evolutionary link between diverse phototransducing proteins". Trends in Biochemical Sciences 22 (12): 458–9. December 1997. doi:10.1016/S0968-0004(97)01148-1. PMID 9433123. 
  3. "Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor". The EMBO Journal 19 (20): 5288–99. October 2000. doi:10.1093/emboj/19.20.5288. PMID 11032796. 
  4. "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. March 2000. doi:10.1073/pnas.050585197. PMID 10725373. Bibcode2000PNAS...97.3702F. 
  5. "Structural and biochemical aspects of tandem GAF domains". CGMP: Generators, Effectors and Therapeutic Implications. Handbook of Experimental Pharmacology. 191. 2009. pp. 93–109. doi:10.1007/978-3-540-68964-5_6. ISBN 978-3-540-68960-7.