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1an1

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Revision as of 10:31, 15 November 2017

LEECH-DERIVED TRYPTASE INHIBITOR/TRYPSIN COMPLEX

Structural highlights

1an1 is a 2 chain structure with sequence from Hirme and Pig. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Activity:	Trypsin, with EC number 3.4.21.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LDTI_HIRME] Acts as an inhibitor of human tryptase, trypsin and chymotrypsin. Probably acts to block host defense mechanisms.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

BACKGROUND: Tryptase is a trypsin-like serine proteinase stored in the cytoplasmic granules of mast cells, which has been implicated in a number of mast cell related disorders such as asthma and rheumatoid arthritis. Unlike almost all other serine proteinases, tryptase is fully active in plasma and in the extracellular space, as there are no known natural inhibitors of tryptase in humans. Leech-derived tryptase inhibitor (LDTI), a protein of 46 amino acids, is the first molecule found to bind tightly to and specifically inhibit human tryptase in the nanomolar range. LDTI also inhibits trypsin and chymotrypsin with similar affinities. The structure of LDTI in complex with an inhibited proteinase could be used as a template for the development of low molecular weight tryptase inhibitors. RESULTS: The crystal structure of the complex between trypsin and LDTI was solved at 2.0 A resolution and a model of the LDTI-tryptase complex was created, based on this X-ray structure. LDTI has a very similar fold to the third domain of the turkey ovomucoid inhibitor. LDTI interacts with trypsin almost exclusively through its binding loop (residues 3-10) and especially through the sidechain of the specificity residue Lys8. Our modeling studies indicate that these interactions are maintained in the LDTI-tryptase complex. CONCLUSIONS: The insertion of nine residues after residue 174 in tryptase, relative to trypsin and chymotrypsin, prevents inhibition by other trypsin inhibitors and is certainly responsible for the higher specificity of tryptase relative to trypsin. In LDTI, the disulfide bond between residues 4 and 25 causes a sharp turn from the binding loop towards the N terminus, holding the N terminus away from the 174 loop of tryptase.

Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LDTI-tryptase system.,Di Marco S, Priestle JP Structure. 1997 Nov 15;5(11):1465-74. PMID:9384562^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Di Marco S, Priestle JP. Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LDTI-tryptase system. Structure. 1997 Nov 15;5(11):1465-74. PMID:9384562

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1an1"

@@ Line 1: / Line 1: @@
 ==LEECH-DERIVED TRYPTASE INHIBITOR/TRYPSIN COMPLEX==
 <StructureSection load='1an1' size='340' side='right' caption='[[1an1]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAS:D-ASPARTIC+ACID'>DAS</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1an1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1an1 OCA], [http://pdbe.org/1an1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1an1 RCSB], [http://www.ebi.ac.uk/pdbsum/1an1 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1an1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1an1 OCA], [http://pdbe.org/1an1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1an1 RCSB], [http://www.ebi.ac.uk/pdbsum/1an1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1an1 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 31: / Line 32: @@
 ==See Also==
-*[[Trypsin|Trypsin]]
 *[[Tryptase inhibitor|Tryptase inhibitor]]
 == References ==

1an1

From Proteopedia

Revision as of 10:31, 15 November 2017

LEECH-DERIVED TRYPTASE INHIBITOR/TRYPSIN COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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