1fe5

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{{STRUCTURE_1fe5| PDB=1fe5 | SCENE= }}
{{STRUCTURE_1fe5| PDB=1fe5 | SCENE= }}
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'''SEQUENCE AND CRYSTAL STRUCTURE OF A BASIC PHOSPHOLIPASE A2 FROM COMMON KRAIT (BUNGARUS CAERULEUS) AT 2.4 RESOLUTION: IDENTIFICATION AND CHARACTERIZATION OF ITS PHARMACOLOGICAL SITES.'''
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===SEQUENCE AND CRYSTAL STRUCTURE OF A BASIC PHOSPHOLIPASE A2 FROM COMMON KRAIT (BUNGARUS CAERULEUS) AT 2.4 RESOLUTION: IDENTIFICATION AND CHARACTERIZATION OF ITS PHARMACOLOGICAL SITES.===
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==Overview==
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This is the first phospholipase A2 (PLA2) structure from the family of kraits. The protein was isolated from Bungarus caeruleus (common krait) and the primary sequence was determined using cDNA approach. Three-dimensional structure of this presynaptic neurotoxic PLA2 from group I has been determined by molecular replacement method using the model of PLA2 component of beta2-bungarotoxin (Bungarus multicinctus) and refined using CNS package to a final R-factor of 20.1 % for all the data in resolution range 20.0-2.4 A. The final refined model comprises 897 protein atoms and 77 water molecules. The overall framework of krait phospholipase A2 with three long helices and two short antiparallel beta-strands is extremely similar to those observed for other group I PLA2s. However, the critical parts of PLA2 folding are concerned with its various functional loops. The conformations of these loops determine the efficiency of enzyme action and presence/absence of various pharmacological functions. In the present structure calcium-binding loop is occupied by a sodium ion with a 7-fold co-ordination. The conformation of loop 55-75 in krait PLA2 corresponds to a very high activity of the enzyme. A comparison of its sequence with multimeric PLA2s clearly shows the absence of critical residues such as Tyr3, Trp61 and Phe64, which are involved in the multimerization of PLA2 molecules. The protein shows anticoagulant and neurotoxic activities.
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(as it appears on PubMed at http://www.pubmed.gov), where 11286555 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11286555}}
==About this Structure==
==About this Structure==
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[[Category: Presynaptic neurotoxin]]
[[Category: Presynaptic neurotoxin]]
[[Category: X-ray structure]]
[[Category: X-ray structure]]
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Revision as of 00:07, 1 July 2008

Image:1fe5.png

Template:STRUCTURE 1fe5

SEQUENCE AND CRYSTAL STRUCTURE OF A BASIC PHOSPHOLIPASE A2 FROM COMMON KRAIT (BUNGARUS CAERULEUS) AT 2.4 RESOLUTION: IDENTIFICATION AND CHARACTERIZATION OF ITS PHARMACOLOGICAL SITES.

Template:ABSTRACT PUBMED 11286555

About this Structure

1FE5 is a Single protein structure of sequence from Bungarus caeruleus. Full crystallographic information is available from OCA.

Reference

Sequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites., Singh G, Gourinath S, Sharma S, Paramasivam M, Srinivasan A, Singh TP, J Mol Biol. 2001 Apr 6;307(4):1049-59. PMID:11286555

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