Its upper half is rounded and indistinctly marked, serving for the attachment of the lower part of the insertion of the teres minor muscle, and below this giving origin to the lateral head of the triceps brachii muscle; its center is traversed by a broad but shallow oblique depression, the spiral groove (musculospiral groove). The radial nerve runs in the spiral groove. Its lower part forms a prominent, rough margin, a little curved from backward, forward the lateral supracondylar ridge, which presents an anterior lip for the origin of the brachioradialis muscle above, and extensor carpi radialis longus muscle above, a posterior lip for the triceps brachii muscle, and an intermediate ridge for the attachment of the lateral intermuscular septum. Medial: the medial border extends from the lesser tubercle to the medial epicondyle. Its upper third consists of a prominent ridge, the crest of the lesser tubercle, which gives insertion to the tendon of the teres major muscle. About its center is a slight impression for the insertion of the coracobrachialis muscle, and just below this is the entrance of the nutrient canal, directed downward; sometimes there is a second nutrient canal at the commencement of the radial sulcus.
The most prevalent ACHM3 mutation, T383IfsX12, results in a non-functional truncated protein that does not properly traffic to the cell membrane.The three missense mutations that have received further study show a number of aberrant properties, with one underlying theme. The R403Q mutation, which lies in the pore region of the channel, results in an increase in outward current rectification, versus the largely linear current-voltage relationship of wild-type channels, concomitant with an increase in cGMP affinity. The other mutations show either increased (S435F) or decreased (F525N) surface expression but also with increased affinity for cAMP and cGMP. It is the increased affinity for cGMP and cAMP in these mutants that is likely the disorder-causing change. Such increased affinity will result in channels that are insensitive to the slight concentration changes of cGMP due to light input into the retina. ACHM4
Upon activation by light, cone opsin causes the exchange of GDP for GTP in the guanine nucleotide binding protein (G-protein) α-transducing activity polypeptide 2 (GNAT2). This causes the release of the activated α-subunit from the inhibitory β/γ-subunits. This α-subunit then activates a phosphodiesterase that catalyzes the conversion of cGMP to GMP, thereby reducing current through CNG3 channels. As this process is absolutely vital for proper color processing it is not surprising that mutations in GNAT2 lead to achromatopsia. The known mutations in this gene, all result in truncated proteins. Presumably, then, these proteins are non-functional and, consequently, cone opsin that has been activated by light does not lead to altered cGMP levels or photoreceptor membrane hyperpolarization.