DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Nature 2008 imex curation Moldoveanu T., Gehring K., Green DR. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Moldoveanu T., Gehring K., Green DR. DIP original experiment: DIP-249978X Nature 2008 IMEx Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Nature 2008 imex curation Moldoveanu T., Gehring K., Green DR. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Moldoveanu T., Gehring K., Green DR. DIP original experiment: DIP-249976X Nature 2008 IMEx Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Nature 2008 imex curation Moldoveanu T., Gehring K., Green DR. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Moldoveanu T., Gehring K., Green DR. DIP original experiment: DIP-249977X Nature 2008 IMEx Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Nature 2008 imex curation Moldoveanu T., Gehring K., Green DR. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Moldoveanu T., Gehring K., Green DR. DIP original experiment: DIP-249975X Nature 2008 IMEx Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. cpns1_rat Calpain small subunit 1 Calcium-dependent protease small subunit 1 Calcium-dependent protease small subunit Calpain regulatory subunit Calcium-activated neutral proteinase small subunit Capns1 Capn4 Css1 protein protein rat Rattus norvegicus (Rat) Rat MFLVNSFLKGGGGGGGGGGLGGGLGNVLGGLISGAAGGGGGGGGGGGMGLGGGGGGGGTAMRILGGVISAISEAAAQYNPEPPPPRSHYSNIEANESEEERQFRKLFVQLAGDDMEVSATELMNILNKVVTRHPDLKTDGFGIDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKKWQGIYKRFDTDRSGTIGSNELPGAFEAAGFHLNQHIYSMIIRRYSDETGNMDFDNFISCLVRLDAMFRAFRSLDKNGTGQIQVNIQEWLQLTMYS DIP protein Q64537 original sequence version: 105 63609614CD4D3EB7 can2_rat Calpain-2 catalytic subunit Capn2 Calpain-2 large subunit Calcium-activated neutral proteinase 2 Calpain M-type Millimolar-calpain protein protein rat Rattus norvegicus (Rat) Rat MAGIAMKLAKDREAAEGLGSHERAIKYLNQDYETLRNECLEAGALFQDPSFPALPSSLGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLDQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELRKPPPNLFKIIQKALEKGSLLGCSIDITSAADSEAVTYQKLVKGHAYSVTGAEEVESSGSLQKLIRIRNPWGQVEWTGKWNDNCPSWNTVDPEVRANLTERQEDGEFWMSFSDFLRHYSRLEICNLTPDTLTCDSYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDDEDGERGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELTGQTNIHLSKNFFLTTRARERSDTFINLREVLNRFKLPPGEYVLVPSTFEPHKNGDFCIRVFSEKKADYQTVDDEIEANIEEIEANEEDIGDGFRRLFAQLAGEDAEISAFELQTILRRVLAKREDIKSDGFSIETCKIMVDMLDEDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHQVIVARFADDELIIDFDNFVRCLVRLEILFKIFKQLDPENTGTIQLDLISWLSFSVL DIP protein Q07009 original sequence version: 129 296B0DC3BEEF5B90 ical_rat Calpastatin Cast Calpain inhibitor protein protein rat Rattus norvegicus (Rat) Rat MSRPGPKPAASSRPRRGAAASHTQEHVNEKNIGSSSKPAEKKGSDEVTASSAATGTSPRMSTTGAKAVKIESEKSQSSEPPVIHEKKPKGKPKEGSEPQTLPKHASDTGSKHAHKEKALSRSNEQIVSEKSSESKTKFQDAPSADGESVAGGVTVATASDKVVVKKKEKKSLTPTLPMESTLNKLSDKSGVNAALDDLIDTLGECEDTNKDDPPYTGPVVLDPMDSTYLEALGIKEGTIPPEYRKLLEKNEAITGPLPDSPKPMGIDHAIDALSSDFTCSSPTGKQTEKEKSTGESSKAQSAGVTRSAVPPQEKKRKVEEEVMNDQALQALSDSLGTRQPDPQSHLRQAKQVKEAKAKEERQEKCGEDEDTVPAEYRLKPAKDKDGKPLLPEPEETSKCLSESELIGELSADFVQPTYQEKPSMPAAKIKKGVVPDDAVETLARSLGTRKEDPEDEKSLVDKVKEKAKEEDHEKLGEKEETIPPDYRLEIVKDKDGKPLLPKEAEEQLPPLSDDFLLDALSQDFSSPANILSLGFEDAKLSAAVSETVSQVPAPSNHTAAPPPGTERRDKELDDALDELSDSLGQRQPDPDENKPLDDKVKEKIKAEHSEKLGERDDTIPPEYRHLLDNDGKDKPEKPLTKNTEKLGQDQDPIDALSEDLDSCPPTTETSQNTTKEKGKKTSSSKASKNEEKTKDSSKKTEEVPKPKVDEDAT DIP protein P27321 original sequence version: 93 DIP protein P27321-1 original sequence version: 62 mint Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue 55505300F59A8DE3 capn2-capns1-6 4 5 unspecified role unspecified role unspecified role unspecified role Region 87-270 Region 87-270 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction capn2-capns1-7 3 7 unspecified role unspecified role unspecified role unspecified role Region 193-278 Region 193-278 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role Region 87-270 Region 87-270 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association capn2-capns1-8 2 7 unspecified role unspecified role unspecified role unspecified role Region 193-278 Region 193-278 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role Region 87-270 Region 87-270 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association capn2-capns1-9 1 7 unspecified role unspecified role unspecified role unspecified role Region 193-278 Region 193-278 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role Region 87-270 Region 87-270 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction