Reentrant loops: Difference between revisions
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Reentrant loops are an important structural motif in alpha-helical transmembrane proteins. A reentrant loop is a structural motif that goes only halfway through the membrane and then turns back to the side from which it originates. <ref>PMID:20544377</ref></br> | |||
<ref>PMID:20544377</ref></br> | They were first seen in the aquaporin water channel. <ref>PMID: 17579561</ref>. | ||
<ref>PMID: 17579561</ref> | In aquaporin, two re-entrant helix-forming loops stack on top of each other <ref>PMID: 35163313</ref>. | ||
<ref>PMID: 35163313</ref> | |||
Reentrant loops seem to be most commonly found in ion and water channel proteins. | |||
== See also == | == See also == | ||
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*[[Aquaporin]] | *[[Aquaporin]] | ||
*[[1bl8]] | *[[1bl8]] | ||
* [[1XFH]] - "The glutamate transporter homolog (1XFH) contains both disrupted | * [[1XFH]] - "The glutamate transporter homolog (1XFH) contains both disrupted transmembrane helices and reentrant loops." | ||
transmembrane helices and reentrant loops." | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 18:44, 27 February 2026
Reentrant loops are an important structural motif in alpha-helical transmembrane proteins. A reentrant loop is a structural motif that goes only halfway through the membrane and then turns back to the side from which it originates. [1]
They were first seen in the aquaporin water channel. [2].
In aquaporin, two re-entrant helix-forming loops stack on top of each other [3].
Reentrant loops seem to be most commonly found in ion and water channel proteins.
See also
- Aquaporin
- 1bl8
- 1XFH - "The glutamate transporter homolog (1XFH) contains both disrupted transmembrane helices and reentrant loops."
References
- ↑ Yan C, Luo J. An analysis of reentrant loops. Protein J. 2010 Jul;29(5):350-4. PMID:20544377 doi:10.1007/s10930-010-9259-z
- ↑ Elofsson A, von Heijne G. Membrane protein structure: prediction versus reality. Annu Rev Biochem. 2007;76:125-40. PMID:17579561 doi:10.1146/annurev.biochem.76.052705.163539
- ↑ Wagner K, Unger L, Salman MM, Kitchen P, Bill RM, Yool AJ. Signaling Mechanisms and Pharmacological Modulators Governing Diverse Aquaporin Functions in Human Health and Disease. Int J Mol Sci. 2022 Jan 26;23(3):1388. PMID:35163313 doi:10.3390/ijms23031388
