Key result
A structural motif (Gly503-Arg-Gly-Ser-Asn-Tyr-Gly509) was identified as the ATP-regulatory module of ANF-dependent guanylate cyclase, which binds ATP and amplifies cyclase activity.
Identifies the specific structural motif (Gly503-Gly509) acting as the ATP-regulatory module in ANF-dependent guanylate cyclase, crucial for ANF signaling.
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No immediate clinical implications for ANF signaling; leaves open motif validation in human cardiovascular models.
Atrial natriuretic factor (ANF)-dependent guanylate cyclase is a single-chain transmembrane-spanning protein, containing an ANF receptor and having catalytic activity. ANF binding to the receptor domain activates the catalytic domain, generating the second messenger cyclic GMP. Obligatory in this activation process is an intervening step regulated by ATP, but its mechanism is not known. Through a programme of site-directed and deletion mutagenesis/expression studies, we report herein the identity of a structural motif (Gly503-Arg-Gly-Ser-Asn-Tyr-Gly509) that binds ATP and amplifies the ANF-dependent cyclase activity; this, therefore, represents an ATP-regulatory module (ARM) of the enzyme, which plays a pivotal role in ANF signalling.
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Goraczniak et al. (1992) studied this question. Site-directed and deletion mutagenesis was evaluated on Identification of ATP-regulatory module. A structural motif (Gly503-Arg-Gly-Ser-Asn-Tyr-Gly509) was identified as the ATP-regulatory module of ANF-dependent guanylate cyclase, which binds ATP and amplifies cyclase activity.
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