Inositol polyphosphate 5-phosphatase OCRL: Difference between revisions
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== OCRL1 == | == OCRL1 == | ||
=== Domains === | === Domains === | ||
The 901 amino acid long OCRL1 is composed of multiple domains which enable it to interact with various partners. OCRL1 consists of an N-terminus '''pleckstrin homology (PH)''' domain without a basic patch required for phosphoinositide recognition and binding. On the other hand, it contains a loop outside of the domain fold that is involved in OCRL1 recruitment to endocytic clathrin-coated pits. <ref name="PH">PMID: 19536138</ref> | The 901 amino acid long '''OCRL1''' or '''Lowe oculocerebronal syndrome protein''' is composed of multiple domains which enable it to interact with various partners. OCRL1 consists of an N-terminus '''pleckstrin homology (PH)''' domain without a basic patch required for phosphoinositide recognition and binding. On the other hand, it contains a loop outside of the domain fold that is involved in OCRL1 recruitment to endocytic clathrin-coated pits. <ref name="PH">PMID: 19536138</ref> | ||
PH domain is followed by one of the major conserved domains of OCRL1 which is a central '''5-phosphatase (5P) domain''', in which two characteristic motifs are present (WXGDXN(F/Y)R and P(A/S)W(C/T)DRIL separated by 60-75 amino acids (AAs)). These play an important role in both substrate binding and catalysis.<ref name="OCRL">PMID: 16101675</ref> This domain has a Dnase I-like fold. <ref name="IP5">PMID: 22381590</ref> | PH domain is followed by one of the major conserved domains of OCRL1 which is a central '''5-phosphatase (5P) domain''', in which two characteristic motifs are present (WXGDXN(F/Y)R and P(A/S)W(C/T)DRIL separated by 60-75 amino acids (AAs)). These play an important role in both substrate binding and catalysis.<ref name="OCRL">PMID: 16101675</ref> This domain has a Dnase I-like fold. <ref name="IP5">PMID: 22381590</ref> | ||