8d1m

hBest1 Ca2+-unbound closed statehBest1 Ca2+-unbound closed state

Structural highlights

8d1m is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.11Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

BEST1_HUMAN Nanophthalmos;Adult-onset foveomacular vitelliform dystrophy;Best vitelliform macular dystrophy;MRCS syndrome;Autosomal recessive bestrophinopathy;Autosomal dominant vitreoretinochoroidopathy;Retinitis pigmentosa. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.

Function

BEST1_HUMAN Forms calcium-sensitive chloride channels. Highly permeable to bicarbonate.^[1] ^[2] ^[3]

References

↑ Sun H, Tsunenari T, Yau KW, Nathans J. The vitelliform macular dystrophy protein defines a new family of chloride channels. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):4008-13. doi: 10.1073/pnas.052692999. PMID:11904445 doi:http://dx.doi.org/10.1073/pnas.052692999
↑ Tsunenari T, Sun H, Williams J, Cahill H, Smallwood P, Yau KW, Nathans J. Structure-function analysis of the bestrophin family of anion channels. J Biol Chem. 2003 Oct 17;278(42):41114-25. doi: 10.1074/jbc.M306150200. Epub 2003, Aug 7. PMID:12907679 doi:http://dx.doi.org/10.1074/jbc.M306150200
↑ Qu Z, Hartzell HC. Bestrophin Cl- channels are highly permeable to HCO3-. Am J Physiol Cell Physiol. 2008 Jun;294(6):C1371-7. doi:, 10.1152/ajpcell.00398.2007. Epub 2008 Apr 9. PMID:18400985 doi:http://dx.doi.org/10.1152/ajpcell.00398.2007

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OCA

[1] Sun H, Tsunenari T, Yau KW, Nathans J. The vitelliform macular dystrophy protein defines a new family of chloride channels. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):4008-13. doi: 10.1073/pnas.052692999. PMID:11904445 doi:http://dx.doi.org/10.1073/pnas.052692999

[2] Tsunenari T, Sun H, Williams J, Cahill H, Smallwood P, Yau KW, Nathans J. Structure-function analysis of the bestrophin family of anion channels. J Biol Chem. 2003 Oct 17;278(42):41114-25. doi: 10.1074/jbc.M306150200. Epub 2003, Aug 7. PMID:12907679 doi:http://dx.doi.org/10.1074/jbc.M306150200

[3] Qu Z, Hartzell HC. Bestrophin Cl- channels are highly permeable to HCO3-. Am J Physiol Cell Physiol. 2008 Jun;294(6):C1371-7. doi:, 10.1152/ajpcell.00398.2007. Epub 2008 Apr 9. PMID:18400985 doi:http://dx.doi.org/10.1152/ajpcell.00398.2007

[1]

[2]

[3]

8d1m

hBest1 Ca2+-unbound closed statehBest1 Ca2+-unbound closed state

Structural highlights

Disease

Function

See Also

References

Contents

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8d1m

hBest1 Ca2+-unbound closed statehBest1 Ca2+-unbound closed state

Structural highlights

Disease

Function

See Also

References

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