Cyclic nucleotide-binding ___domain

Proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural ___domain of about 120 residues. The best studied of these proteins is the prokaryotic catabolite gene activator (also known as the cAMP receptor protein) (gene crp) where such a ___domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. There are six invariant amino acids in this ___domain, three of which are glycine residues that are thought to be essential for maintenance of the structural integrity of the beta-barrel. cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding ___domain. The cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the ___domain. The cGPK's are single chain enzymes that include the two copies of the ___domain in their N-terminal section. Vertebrate cyclic nucleotide-gated ion-channels also contain this ___domain. Two such cations channels have been fully characterized, one is found in rod cells where it plays a role in visual signal transduction.

Cyclic nucleotide-binding ___domain
Structure of a CAP-DNA complex.[1]
Identifiers
SymbolcNMP_binding
PfamPF00027
InterProIPR000595
SMARTSM00100
PROSITEPDOC00691
SCOP21cgp / SCOPe / SUPFAM
CDDcd00038
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1o7fA:375-462 2apk :153-242 1kmwR:154-243

1kmuR:154-243 1cx4A:170-259 1rl3A:153-238 1ne6A:153-238 1ne4A:153-238 1rgs :153-238 1apk :153-238 1pvkA:153-238 1u7eB:153-238 2bpk :275-372 1bpk :271-362 1q43A:535-620 1q5oA:535-620 1q3eA:535-620 1vp6C:253-336 1u12B:253-336 1i6xA:21-112 1hw5A:21-112 1j59B:21-112 1o3sA:21-112 1g6nB:21-112 1lb2A:21-112 1cgpB:21-112 1ruoB:21-112 2cgpA:21-112 1o3rA:21-112 1i5zB:21-112 1o3tA:21-112 1runA:21-112 1o3qA:21-112

1ft9A:25-107 1o5lA:12-103 1wgpA:532-632

Human proteins containing this ___domain

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CNBD1; CNGA1; CNGA2; CNGA3; CNGB1; CNGB3; HCN1; HCN2; HCN3; HCN4; KCNH1; KCNH2; KCNH3; KCNH4; KCNH5; KCNH6; KCNH7; KCNH8; PNPLA6; PNPLA7; PRKAR1A; PRKAR1B; PRKAR2A; PRKAR2B; PRKG1; PRKG2; RAPGEF2; RAPGEF3; RAPGEF4; RAPGEF6; RCNC2; SLC9A10; SLC9A11;

References

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  1. ^ Schultz SC, Shields GC, Steitz TA (August 1991). "Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees". Science. 253 (5023): 1001–7. Bibcode:1991Sci...253.1001S. doi:10.1126/science.1653449. PMID 1653449. S2CID 19723922. Archived from the original on 2024-05-02. Retrieved 2020-09-11.

Further reading

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This article incorporates text from the public ___domain Pfam and InterPro: IPR000595