Structural highlights
Disease
[RAB28_HUMAN] Cone rod dystrophy. The disease is caused by mutations affecting the gene represented in this entry.[1]
Function
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Rab GTPases are essential regulators of membrane trafficking. We report crystal structures of Rab28 in the active (GppNHp-bound) and inactive (GDP-3'P-bound) forms at 1.5 and 1.1A resolution. Rab28 is a distant member of the Rab family. While the overall fold of Rab28 resembles that of other Rab GTPases, it undergoes a larger nucleotide-dependent conformational change than other members of this family. Added flexibility resulting from a double-glycine motif at the beginning of switch 2 might partially account for this observation. The double-glycine motif, which is conserved in the Arf family, only occurs in Rab28 and Rab7B of the Rab family, and may have a profound effect on their catalytic activities.
Large nucleotide-dependent conformational change in Rab28.,Lee SH, Baek K, Dominguez R FEBS Lett. 2008 Dec 10;582(29):4107-11. Epub 2008 Nov 19. PMID:19026641[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roosing S, Rohrschneider K, Beryozkin A, Sharon D, Weisschuh N, Staller J, Kohl S, Zelinger L, Peters TA, Neveling K, Strom TM, van den Born LI, Hoyng CB, Klaver CC, Roepman R, Wissinger B, Banin E, Cremers FP, den Hollander AI. Mutations in RAB28, encoding a farnesylated small GTPase, are associated with autosomal-recessive cone-rod dystrophy. Am J Hum Genet. 2013 Jul 11;93(1):110-7. doi: 10.1016/j.ajhg.2013.05.005. Epub, 2013 Jun 6. PMID:23746546 doi:http://dx.doi.org/10.1016/j.ajhg.2013.05.005
- ↑ Lee SH, Baek K, Dominguez R. Large nucleotide-dependent conformational change in Rab28. FEBS Lett. 2008 Dec 10;582(29):4107-11. Epub 2008 Nov 19. PMID:19026641 doi:10.1016/j.febslet.2008.11.008
