KH domain

KH domain
KH domain
Identifiers
Symbol	KH_2
Pfam	PF07650
Pfam clan	CL0007
ECOD	327.11.1
InterPro	IPR004044
SMART	KH
PROSITE	PS50823
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1ega, 1fjg, 1gix, 1hnw, 1hnx, 1hnz, 1hr0, 1i94, 1i95, 1i96, 1i97, 1ibk, 1ibl, 1ibm, 1j5e, 1n32, 1n33, 1n34, 1n36, 1vs5, 1vs7, 1wf3, 1wh9, 1xmo, 1xmq, 1xnq, 1xnr, 1yl4, 2avy, 2aw7, 2b64, 2b9m, 2b9o, 2e5l, 2f4v, 2hgi, 2hgp, 2hgr, 2hhh, 2i2p, 2i2u, 2j00, 2j02, 2ow8, 2qal, 2qan, 2qb9, 2qbb, 2qbd, 2qbf, 2qbh, 2qbj, 2qnh, 2qou, 2qow, 2qoy, 2qp0, 2uu9, 2uua, 2uub, 2uuc, 2uxb, 2uxc, 2uxd, 2v46, 2v48, 2vho, 2vhp, 2vqe, 2vqf, 2z4k, 2z4m, 3d5a, 3d5c, 3df1, 3df3, 3f1e, 3f1g

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1dt4, 1dtj, 1e3h, 1e3p, 1ec6, 1j4w, 1j5k, 1k1g, 1khm, 1tua, 1vig, 1vih, 1we8, 1wvn, 1x4m, 1x4n, 1ztg, 1zzi, 1zzj, 1zzk, 2axy, 2ba0, 2bl5, 2cpq, 2cte, 2ctf, 2ctj, 2ctk, 2ctl, 2ctm, 2fmr, 2je6, 2jea, 2p2r, 2pqu, 2py9, 2z0s

KH domain
KH domain
	Structure of a KH domain from the human protein vigilin.
Identifiers
Symbol	KH_1
Pfam	PF00013
Pfam clan	CL0007
ECOD	327.11.2
InterPro	IPR004088
SMART	KH
SCOP2	1vig / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1dt4, 1dtj, 1e3h, 1e3p, 1ec6, 1j4w, 1j5k, 1k1g, 1khm, 1tua, 1vig, 1vih, 1we8, 1wvn, 1x4m, 1x4n, 1ztg, 1zzi, 1zzj, 1zzk, 2axy, 2ba0, 2bl5, 2cpq, 2cte, 2ctf, 2ctj, 2ctk, 2ctl, 2ctm, 2fmr, 2je6, 2jea, 2p2r, 2pqu, 2py9, 2z0s

The K Homology (KH) domain is a protein domain that was first identified in the human heterogeneous nuclear ribonucleoprotein (hnRNP) K. An evolutionarily conserved sequence of around 70 amino acids, the KH domain is present in a wide variety of nucleic acid-binding proteins. The KH domain binds RNA, and can function in RNA recognition.^[1] It is found in multiple copies in several proteins, where they can function cooperatively or independently. For example, in the AU-rich element RNA-binding protein KSRP, which has 4 KH domains, KH domains 3 and 4 behave as independent binding modules to interact with different regions of the AU-rich RNA targets.^[1] The solution structure of the first KH domain of FMR1 and of the C-terminal KH domain of hnRNP K determined by nuclear magnetic resonance (NMR) revealed a beta-alpha-alpha-beta-beta-alpha structure.^[2]^[3] Autoantibodies to NOVA1, a KH domain protein, cause paraneoplastic opsoclonus ataxia. The KH domain is found at the N-terminus of the ribosomal protein S3. This domain is unusual in that it has a different fold compared to the normal KH domain.^[4]

^ ^a ^b García-Mayoral MF, Hollingworth D, Masino L, et al. (April 2007). "The structure of the C-terminal KH domains of KSRP reveals a noncanonical motif important for mRNA degradation" (PDF). Structure. 15 (4): 485–98. doi:10.1016/j.str.2007.03.006. PMID 17437720.
^ Musco G, Kharrat A, Stier G, et al. (September 1997). "The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome". Nat. Struct. Biol. 4 (9): 712–6. doi:10.1038/nsb0997-712. PMID 9302998. S2CID 11166126.
^ Baber JL, Libutti D, Levens D, Tjandra N (June 1999). "High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor". J. Mol. Biol. 289 (4): 949–62. doi:10.1006/jmbi.1999.2818. PMID 10369774.
^ Grishin NV (February 2001). "KH domain: one motif, two folds". Nucleic Acids Res. 29 (3): 638–43. doi:10.1093/nar/29.3.638. PMC 30387. PMID 11160884.

[pmid17437720-1] García-Mayoral MF, Hollingworth D, Masino L, et al. (April 2007). "The structure of the C-terminal KH domains of KSRP reveals a noncanonical motif important for mRNA degradation" (PDF). Structure. 15 (4): 485–98. doi:10.1016/j.str.2007.03.006. PMID 17437720.

[pmid9302998-2] Musco G, Kharrat A, Stier G, et al. (September 1997). "The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome". Nat. Struct. Biol. 4 (9): 712–6. doi:10.1038/nsb0997-712. PMID 9302998. S2CID 11166126.

[pmid10369774-3] Baber JL, Libutti D, Levens D, Tjandra N (June 1999). "High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor". J. Mol. Biol. 289 (4): 949–62. doi:10.1006/jmbi.1999.2818. PMID 10369774.

[pmid11160884-4] Grishin NV (February 2001). "KH domain: one motif, two folds". Nucleic Acids Res. 29 (3): 638–43. doi:10.1093/nar/29.3.638. PMC 30387. PMID 11160884.

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