KV1

Tomb KV1, located in the Valley of the Kings in Egypt, was used for the burial of Pharaoh Ramesses VII of the Twentieth Dynasty. Although it has been open since antiquity, it was only properly investigated and cleared by Edwin Brock in 1984 and 1985. The single corridor tomb itself is located in Luxor's West Bank, and is small in comparison to other tombs of the twentieth dynasty.

Tomb layout

Typical of tombs from this period, KV1 is laid out in along a straight axis. The successors of Ramesses III constructed tombs that had followed this pattern and were all decorated in much the same manner as each other. It consists of four major parts: the entrance, a passageway, the burial chamber containing the sarcophagus, and a final smaller room at the end.

Ramesses VII was in the seventh year of his reign when he died. There is evidence that the room that ended up being the burial chamber was expanded from its original design as a corridor, and work on a subsequent room at the end of the tomb was halted.

Kv1.1

Potassium voltage-gated channel subfamily A member 1 also known as K_v1.1 is a shaker related voltage-gated potassium channel that in humans is encoded by the KCNA1 gene. The Isaacs syndrome is a result of an autoimmune reaction against the K_v1.1 ion channel.

Genomics

The gene is located on the Watson (plus) strand of the short arm of chromosome 12 (12p13.32). The gene itself is 8,348 bases in length and encodes a protein of 495 amino acids (predicted molecular weight 56.466 kiloDaltons).

Alternative names

The recommended name for this protein is potassium voltage-gated channel subfamily A member 1 but a number of alternatives have been used in the literature including HuK1 (human K⁺ channel I), RBK1 (rubidium potassium channel 1), MBK (mouse brain K⁺ channel), voltage gated potassium channel HBK1, voltage gated potassium channel subunit K_v1.1, voltage-gated K⁺ channel HuKI and AEMK (associated with myokymia with periodic ataxia).

Structure

The protein is believed to have six domains (S1-S6) with the loop between S5 and S6 forming the channel pore. This region also has a conserved selectivity filter motif. The functional channel is a homotetramer. The N-terminus of the protein associates with β subunits. These subunits regulate channel inactivation as well as its expression. The C-terminus is associated with a PDZ domain protein involved in channel targeting.