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| | {{STRUCTURE_1bjr| PDB=1bjr | SCENE= }} | | {{STRUCTURE_1bjr| PDB=1bjr | SCENE= }} |
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| - | '''COMPLEX FORMED BETWEEN PROTEOLYTICALLY GENERATED LACTOFERRIN FRAGMENT AND PROTEINASE K'''
| + | ===COMPLEX FORMED BETWEEN PROTEOLYTICALLY GENERATED LACTOFERRIN FRAGMENT AND PROTEINASE K=== |
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| - | ==Overview==
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| - | Lactoferrin is an iron binding glycoprotein with a molecular weight of 80 kDa. The molecule is divided into two lobes representing the N-terminal and C-terminal halves of the polypeptide chain, each containing an iron binding site. The serine proteinases such as trypsin, chymotrypsin, and pepsin hydrolyze lactoferrin into two unequal halves while proteinase K divides this protein into two equal halves. In the first step of hydrolysis by proteinase K, the C- and N-lobes, each having a molecular weight of approximately 40 kDa, are generated. In the next step, the lobes are further hydrolyzed into small molecular weight peptides. The proteinase K isolated from the hydrolyzed product does not show enzymatic activity suggesting that the enzyme is inhibited. Furthermore, the hydrolysis experiments on N-lobe and C-lobe showed that the inhibitory fragment came from the C-lobe. The purified lactoferrin fragment was found to be a decapeptide with an amino acid sequence of H2N-Val-Ala-Gln-Gly-Ala-Ala-Gly-Leu-Ala-COOH. The complex formed between proteinase K and lactoferrin fragment was crystallized by microdialysis. The crystals belonged to the monoclinic space group P2(1) with cell dimensions a = 44.4 A, b = 38.6 A, c = 79.2 A, beta = 105.8 degrees and Z = 2. The crystal structure has been determined at 2.4 A resolution. It has been refined to an R factor of 0.163 for 9044 reflections. The Lf-fragment forms several intermolecular interactions with proteinase K. The Ser-224 Ogamma and His-57 N epsilon2 move away to a distance of 3.68 A in the complex. In the crystal structure, Gln-3I (I indicates inhibitor i.e., lactoferrin fragment) is involved in a direct intermolecular interaction with a symmetry related proteinase K molecule through a strong hydrogen bond with Asp-254. The mode of intermolecular interactions in the complex conformational features of the enzyme and placement of the fragment with respect to the enzyme resemble with the molecular complex of proteinase K with its natural inhibitor PKI3 from wheat.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9741842}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9741842 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9741842}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lactoferrin]] | | [[Category: Lactoferrin]] |
| | [[Category: Proteinase k]] | | [[Category: Proteinase k]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:36:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:16:36 2008'' |
Revision as of 16:16, 30 June 2008
Template:STRUCTURE 1bjr
COMPLEX FORMED BETWEEN PROTEOLYTICALLY GENERATED LACTOFERRIN FRAGMENT AND PROTEINASE K
Template:ABSTRACT PUBMED 9741842
About this Structure
1BJR is a Single protein structure of sequence from Bubalus bubalis and Engyodontium album. Full crystallographic information is available from OCA.
Reference
Crystal structure of a complex formed between proteolytically-generated lactoferrin fragment and proteinase K., Singh TP, Sharma S, Karthikeyan S, Betzel C, Bhatia KL, Proteins. 1998 Oct 1;33(1):30-8. PMID:9741842
Page seeded by OCA on Mon Jun 30 19:16:36 2008
