1bip

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[[Image:1bip.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1bip| PDB=1bip | SCENE= }}
{{STRUCTURE_1bip| PDB=1bip | SCENE= }}
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'''BIFUNCTIONAL PROTEINASE INHIBITOR TRYPSIN/A-AMYLASE FROM SEEDS OF RAGI (ELEUSINE CORACANA GAERTNERI)'''
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===BIFUNCTIONAL PROTEINASE INHIBITOR TRYPSIN/A-AMYLASE FROM SEEDS OF RAGI (ELEUSINE CORACANA GAERTNERI)===
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==Overview==
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The three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor (RBI) from seeds of ragi (Eleusine coracana Gaertneri) has been determined in solution using multidimensional 1H and 15N NMR spectroscopy. The inhibitor consists of 122 amino acids, with 5 disulfide bridges, and belongs to the plant alpha-amylase/trypsin inhibitor family for which no three-dimensional structures have yet been available. The structure of the inhibitor was determined on the basis of 1131 interresidue interproton distance constraints derived from nuclear Overhauser enhancement measurements and 52 phi angles, supplemented by 9 psi and 51 chi 1 angles. RBI consists of a globular four-helix motif with a simple "up-and-down" topology. The helices are between residues 18-29, 37-51, 58-65, and 87-94. A fragment from Val 67 to Ser 69 and Gln 73 to Glu 75 forms an antiparallel beta-sheet. The fold of RBI represents a new motif among the serine proteinase inhibitors. The trypsin binding loop of RBI adopts the "canonical", substrate-like conformation which is highly conserved among serine proteinase inhibitors. The binding loop is stabilized by the two adjacent alpha-helices 1 and 2. This motif is also novel and not found in known structures of serine proteinase inhibitors. The three-dimensional structure of RBI together with biochemical data suggests the location of the alpha-amylase binding site on the face of the molecule opposite to the site of the trypsin binding loop. The RBI fold should be general for all members of the RBI family because conserved residues among the members of the family from the core of the structure.
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(as it appears on PubMed at http://www.pubmed.gov), where 7599120 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7599120}}
==About this Structure==
==About this Structure==
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1BIP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Eleusine_coracana Eleusine coracana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIP OCA].
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1BIP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Eleusine_coracana Eleusine coracana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIP OCA].
==Reference==
==Reference==
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[[Category: Strobl, S.]]
[[Category: Strobl, S.]]
[[Category: Serine proteinase inhibitor]]
[[Category: Serine proteinase inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:33:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:13:34 2008''

Revision as of 16:13, 30 June 2008

Image:1bip.png

Template:STRUCTURE 1bip

BIFUNCTIONAL PROTEINASE INHIBITOR TRYPSIN/A-AMYLASE FROM SEEDS OF RAGI (ELEUSINE CORACANA GAERTNERI)

Template:ABSTRACT PUBMED 7599120

About this Structure

1BIP is a Single protein structure of sequence from Eleusine coracana. Full experimental information is available from OCA.

Reference

Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy., Strobl S, Muhlhahn P, Bernstein R, Wiltscheck R, Maskos K, Wunderlich M, Huber R, Glockshuber R, Holak TA, Biochemistry. 1995 Jul 4;34(26):8281-93. PMID:7599120

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