Calponin homology domain

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1sjj B:33-136 1tjt A:46-149 1wku A:46-149 1sh5 B:186-293 1sh6 A:186-293 1mb8 A:180-282 1dxx A:16-119 1qag B:32-135 1rt8 A:386-495 1pxy B:393-498 1aoa :121-236 1wyp A:29-132 1h67 A:29-132 1wyn A:29-132 1ujo A:25-138 1wym A:25-137 1wyr A:4-111 1p2x A:42-148 1p5s A:42-148 1bkr A:174-278 1aa2 :174-278 1wyq A:178-281 1bhd A:151-254 1wyl A:509-612 1wjo A:517-624 1wyo A:15-116 1vka B:15-116 1ueg A:15-116 1pa7 A:15-116

Calponin homology (CH) domain
Calponin homology (CH) domain
	Solution structure of calponin homology domain of IQGAP1
Identifiers
Symbol	CH
Pfam	PF00307
InterPro	IPR001715
SMART	CH
PROSITE	PDOC00019
SCOP2	1aoa / SCOPe / SUPFAM
CDD	cd00014
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1sjj B:33-136 1tjt A:46-149 1wku A:46-149 1sh5 B:186-293 1sh6 A:186-293 1mb8 A:180-282 1dxx A:16-119 1qag B:32-135 1rt8 A:386-495 1pxy B:393-498 1aoa :121-236 1wyp A:29-132 1h67 A:29-132 1wyn A:29-132 1ujo A:25-138 1wym A:25-137 1wyr A:4-111 1p2x A:42-148 1p5s A:42-148 1bkr A:174-278 1aa2 :174-278 1wyq A:178-281 1bhd A:151-254 1wyl A:509-612 1wjo A:517-624 1wyo A:15-116 1vka B:15-116 1ueg A:15-116 1pa7 A:15-116

Last updated October 02, 2024

Calponin homology domain (or CH domain) is a family of actin binding domains found in both cytoskeletal proteins and signal transduction proteins.^[2] The domain is about 100 amino acids in length and is composed of four alpha helices.^[3] It comprises the following groups of actin-binding domains:

Actinin-type (including spectrin, fimbrin, ABP-280)
Calponin-type

A comprehensive review of proteins containing this type of actin-binding domains is given in.^[4]

The CH domain is involved in actin binding in some members of the family. However, in calponins there is evidence that the CH domain is not involved in its actin binding activity.^[5] Most proteins have two copies of the CH domain, however some proteins such as calponin and the human vav proto-oncogene ( P15498 ) have only a single copy. The structure of an example CH domain has been determined using X-ray crystallography.^[6]

Examples

Human genes encoding calponin homology domain-containing proteins include:

ACTN1, ACTN2, ACTN3, ACTN4, ARHGEF6, ARHGEF7, ASPM,
CLMN, CNN1, CNN2, CNN3,
DIXDC1, DMD, DST,
EHBP1, EHBP1L1,
FLNA, FLNB, FLNC,
GAS2, GAS2L1, GAS2L2, GAS2L3,
IQGAP1, IQGAP2, IQGAP3,
LCP1, LIMCH1, LMO7, LRCH1, LRCH2, LRCH3, LRCH4,
MACF1, MAPRE1, MAPRE2, MAPRE3, MICAL1, MICAL2, MICAL2PV1, MICAL2PV2, MICAL3, MICALL1, MICALL2,
NAV2, NAV3,
PARVA, PARVB, PARVG, PLEC1, PLS1, PLS3, PP14183,
SMTN, SMTNL2, SPECC1, SPECC1L, SPNB4, SPTB, SPTBN1, SPTBN2, SPTBN4, SPTBN5, SYNE1, SYNE2,
TAGLN, TAGLN2, TAGLN3,
UTRN, and
VAV1, VAV2, VAV3

Related Research Articles

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Utrophin is a protein that in humans is encoded by the UTRN gene. The name is a short form for ubiquitous dystrophin.

<span class="mw-page-title-main">Calponin</span> Calcium binding protein

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<span class="mw-page-title-main">CDC42</span> Protein-coding gene in the species Homo sapiens

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Proto-oncogene vav is a protein that in humans is encoded by the VAV1 gene.

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Calponin 1 is a basic smooth muscle protein that in humans is encoded by the CNN1 gene.

References

↑ PDB: 2RR8 ; Umemoto R, Nishida N, Ogino S, Shimada I (September 2010). "NMR structure of the calponin homology domain of human IQGAP1 and its implications for the actin recognition mode". J. Biomol. NMR. 48 (1): 59–64. doi:10.1007/s10858-010-9434-8. PMID 20644981. S2CID 25649748.
↑ Saraste M, Castresana J (1995). "Does Vav bind to F-actin through a CH domain?". FEBS Lett. 374 (2): 149–151. doi:10.1016/0014-5793(95)01098-Y. PMID 7589522. S2CID 29667309.
↑ Korenbaum, E.; Rivero, F. (Sep 2002). "Calponin homology domains at a glance". J Cell Sci. 115 (Pt 18): 3543–5. CiteSeerX 10.1.1.608.8653 . doi:10.1242/jcs.00003. PMID 12186940. S2CID 38137068.
↑ Hartwig JH (1995). "Actin-binding proteins. 1: Spectrin super family". Protein Prof. 2 (7): 703–800. PMID 7584474.
↑ Gimona M, Mital R (1998). "The single CH domain of calponin is neither sufficient nor necessary for F-actin binding". J. Cell Sci. 111: 1813–1821. PMID 9625744.
↑ Saraste M, Carugo KD, Banuelos S (1997). "Crystal structure of a calponin homology domain". Nat. Struct. Biol. 4 (3): 175–179. doi:10.1038/nsb0397-175. PMID 9164454. S2CID 1428195.

This article incorporates text from the public domain Pfam and InterPro: IPR001715

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[pmid20644981-1] PDB: 2RR8 ; Umemoto R, Nishida N, Ogino S, Shimada I (September 2010). "NMR structure of the calponin homology domain of human IQGAP1 and its implications for the actin recognition mode". J. Biomol. NMR. 48 (1): 59–64. doi:10.1007/s10858-010-9434-8. PMID 20644981. S2CID 25649748.

[PUB00001696-2] Saraste M, Castresana J (1995). "Does Vav bind to F-actin through a CH domain?". FEBS Lett. 374 (2): 149–151. doi:10.1016/0014-5793(95)01098-Y. PMID 7589522. S2CID 29667309.

[Korenbaum-2002-3] Korenbaum, E.; Rivero, F. (Sep 2002). "Calponin homology domains at a glance". J Cell Sci. 115 (Pt 18): 3543–5. CiteSeerX 10.1.1.608.8653 . doi:10.1242/jcs.00003. PMID 12186940. S2CID 38137068.

[PUB00004975-4] Hartwig JH (1995). "Actin-binding proteins. 1: Spectrin super family". Protein Prof. 2 (7): 703–800. PMID 7584474.

[PUB00003095-5] Gimona M, Mital R (1998). "The single CH domain of calponin is neither sufficient nor necessary for F-actin binding". J. Cell Sci. 111: 1813–1821. PMID 9625744.

[PUB00003938-6] Saraste M, Carugo KD, Banuelos S (1997). "Crystal structure of a calponin homology domain". Nat. Struct. Biol. 4 (3): 175–179. doi:10.1038/nsb0397-175. PMID 9164454. S2CID 1428195.

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