Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology

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Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M202327200
P698PubMed publication ID11960990

P50authorChristian CambillauQ5109395
Silvia SpinelliQ28037071
Serge MuyldermansQ39183359
Lode WynsQ48739361
P2093author name stringFrancoise Payan
Aline Desmyter
Marc Lauwereys
P2860cites workCrystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationQ26778405
PROCHECK: a program to check the stereochemical quality of protein structuresQ26778411
A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loopsQ27617837
Camelid heavy-chain variable domains provide efficient combining sites to haptensQ27621499
Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes?Q27625032
Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibodyQ27631669
Lateral recognition of a dye hapten by a llama VHH domainQ27633538
The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor TendamistatQ27730434
The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolutionQ27731333
The crystal structure of a llama heavy chain variable domainQ27733333
Crystal structure of a camel single-domain VH antibody fragment in complex with lysozymeQ27733338
Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complexQ27734356
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical featuresQ27860675
NMRPipe: a multidimensional spectral processing system based on UNIX pipesQ27860859
The CCP4 suite: programs for protein crystallographyQ27861090
The atomic structure of protein-protein recognition sitesQ27861113
Standard conformations for the canonical structures of immunoglobulinsQ28254522
Naturally occurring antibodies devoid of light chainsQ28269589
AMoRe: an automated package for molecular replacementQ29642803
Loss of splice consensus signal is responsible for the removal of the entire C(H)1 domain of the functional camel IGG2A heavy-chain antibodiesQ30766668
The structure of the llama heavy chain constant genes reveals a mechanism for heavy-chain antibody formationQ30803385
Anatomy of the antibody moleculeQ34060425
Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domainsQ34214306
Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chainsQ34662422
Camel single-domain antibody inhibits enzyme by mimicking carbohydrate substrateQ38333730
Camel heavy-chain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoireQ40387210
T-cell receptor structure and TCR complexesQ41685092
Potent enzyme inhibitors derived from dromedary heavy-chain antibodiesQ41782789
Conformations of the third hypervariable region in the VH domain of immunoglobulinsQ47626454
P433issue26
P407language of work or nameEnglishQ1860
P304page(s)23645-50
P577publication date2002-06-28
P1433published inJournal of Biological ChemistryQ867727
P1476titleThree camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology
P478volume277

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